Loading…

Structural stability studies in adhesion molecules—role of cation–π interactions

Cell adhesion molecules are important for their various roles in many cellular events and responses. In the present study, we have analyzed the roles played by cation–π interactions in the structural stability of adhesion molecules. These interactions are mainly formed by long-range contacts. The oc...

Full description

Saved in:

Bibliographic Details
Published in:	Protoplasma 2011-10, Vol.248 (4), p.673-682
Main Authors:	Sophiya, K, Anbarasu, Anand
Format:	Article
Language:	English
Subjects:	adhesion Amino Acid Sequence Amino Acids - chemistry arginine Biomedical and Life Sciences Cations - chemistry cell adhesion Cell Adhesion Molecules - chemistry Cell Biology Computational Biology Conserved Sequence Databases, Protein Life Sciences lysine Original Article Plant Sciences Protein Interaction Mapping Protein Stability Protein Structure, Secondary proteins Sequence Alignment Sequence Analysis, Protein Solvents - chemistry Zoology
Citations:	Items that this one cites Items that cite this one
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

cited_by	cdi_FETCH-LOGICAL-c367t-23c23609586443d61c989a430ee555ae55219aba11737454a427b2a891709cf3
cites	cdi_FETCH-LOGICAL-c367t-23c23609586443d61c989a430ee555ae55219aba11737454a427b2a891709cf3
container_end_page	682
container_issue	4
container_start_page	673
container_title	Protoplasma
container_volume	248
creator	Sophiya, K Anbarasu, Anand
description	Cell adhesion molecules are important for their various roles in many cellular events and responses. In the present study, we have analyzed the roles played by cation–π interactions in the structural stability of adhesion molecules. These interactions are mainly formed by long-range contacts. The occurrence of arginine is higher than lysine to form cation–π interactions. The secondary structure preferences of interacting residues are independent of amino acid class. Cation–π interactions might stabilize the interface between the terminus and core in this class of proteins. The results obtained in the present study will be useful in understanding the contribution of cation–π interactions to the overall stability of adhesion proteins.
doi_str_mv	10.1007/s00709-010-0224-7
format	article
fullrecord	<record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_902085818</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>902085818</sourcerecordid><originalsourceid>FETCH-LOGICAL-c367t-23c23609586443d61c989a430ee555ae55219aba11737454a427b2a891709cf3</originalsourceid><addsrcrecordid>eNp9kE1OwzAQhS0EoqVwADaQHavA-C9xlqjiT6rEoq3EznIcp7hKk2Ini-56B7gXd-hJcJXCks3MaOa9J82H0CWGWwyQ3vlQIIsBQwyEsDg9QkOcYB4nGMgxGgJQGmNB3wbozPslAHAC_BQNCGSpECCGaD5tXafbzqkq8q3KbWXbTZi6whof2TpSxbvxtqmjVVMZ3VXG77ZfLsxRU0ZateG0235-b4O2NU7p_cKfo5NSVd5cHPoIzR4fZuPnePL69DK-n8SaJmkbE6oJTSDjImGMFgnWmcgUo2AM51yFQnCmcoVxSlPGmWIkzYkSGQ5v65KO0E0fu3bNR2d8K1fWa1NVqjZN52UGBAQXgcAI4V6pXeO9M6VcO7tSbiMxyD1L2bOUgaXcs5Rp8Fwd0rt8ZYo_xy-8ICC9wIdTvTBOLpvO1eHhf1Ove1OpGqkWzno5nxLADAAnLGChP6SHilQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>902085818</pqid></control><display><type>article</type><title>Structural stability studies in adhesion molecules—role of cation–π interactions</title><source>Springer Nature</source><creator>Sophiya, K ; Anbarasu, Anand</creator><creatorcontrib>Sophiya, K ; Anbarasu, Anand</creatorcontrib><description>Cell adhesion molecules are important for their various roles in many cellular events and responses. In the present study, we have analyzed the roles played by cation–π interactions in the structural stability of adhesion molecules. These interactions are mainly formed by long-range contacts. The occurrence of arginine is higher than lysine to form cation–π interactions. The secondary structure preferences of interacting residues are independent of amino acid class. Cation–π interactions might stabilize the interface between the terminus and core in this class of proteins. The results obtained in the present study will be useful in understanding the contribution of cation–π interactions to the overall stability of adhesion proteins.</description><identifier>ISSN: 0033-183X</identifier><identifier>EISSN: 1615-6102</identifier><identifier>DOI: 10.1007/s00709-010-0224-7</identifier><identifier>PMID: 20978808</identifier><language>eng</language><publisher>Vienna: Springer-Verlag</publisher><subject>adhesion ; Amino Acid Sequence ; Amino Acids - chemistry ; arginine ; Biomedical and Life Sciences ; Cations - chemistry ; cell adhesion ; Cell Adhesion Molecules - chemistry ; Cell Biology ; Computational Biology ; Conserved Sequence ; Databases, Protein ; Life Sciences ; lysine ; Original Article ; Plant Sciences ; Protein Interaction Mapping ; Protein Stability ; Protein Structure, Secondary ; proteins ; Sequence Alignment ; Sequence Analysis, Protein ; Solvents - chemistry ; Zoology</subject><ispartof>Protoplasma, 2011-10, Vol.248 (4), p.673-682</ispartof><rights>Springer-Verlag 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c367t-23c23609586443d61c989a430ee555ae55219aba11737454a427b2a891709cf3</citedby><cites>FETCH-LOGICAL-c367t-23c23609586443d61c989a430ee555ae55219aba11737454a427b2a891709cf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20978808$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sophiya, K</creatorcontrib><creatorcontrib>Anbarasu, Anand</creatorcontrib><title>Structural stability studies in adhesion molecules—role of cation–π interactions</title><title>Protoplasma</title><addtitle>Protoplasma</addtitle><addtitle>Protoplasma</addtitle><description>Cell adhesion molecules are important for their various roles in many cellular events and responses. In the present study, we have analyzed the roles played by cation–π interactions in the structural stability of adhesion molecules. These interactions are mainly formed by long-range contacts. The occurrence of arginine is higher than lysine to form cation–π interactions. The secondary structure preferences of interacting residues are independent of amino acid class. Cation–π interactions might stabilize the interface between the terminus and core in this class of proteins. The results obtained in the present study will be useful in understanding the contribution of cation–π interactions to the overall stability of adhesion proteins.</description><subject>adhesion</subject><subject>Amino Acid Sequence</subject><subject>Amino Acids - chemistry</subject><subject>arginine</subject><subject>Biomedical and Life Sciences</subject><subject>Cations - chemistry</subject><subject>cell adhesion</subject><subject>Cell Adhesion Molecules - chemistry</subject><subject>Cell Biology</subject><subject>Computational Biology</subject><subject>Conserved Sequence</subject><subject>Databases, Protein</subject><subject>Life Sciences</subject><subject>lysine</subject><subject>Original Article</subject><subject>Plant Sciences</subject><subject>Protein Interaction Mapping</subject><subject>Protein Stability</subject><subject>Protein Structure, Secondary</subject><subject>proteins</subject><subject>Sequence Alignment</subject><subject>Sequence Analysis, Protein</subject><subject>Solvents - chemistry</subject><subject>Zoology</subject><issn>0033-183X</issn><issn>1615-6102</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNp9kE1OwzAQhS0EoqVwADaQHavA-C9xlqjiT6rEoq3EznIcp7hKk2Ini-56B7gXd-hJcJXCks3MaOa9J82H0CWGWwyQ3vlQIIsBQwyEsDg9QkOcYB4nGMgxGgJQGmNB3wbozPslAHAC_BQNCGSpECCGaD5tXafbzqkq8q3KbWXbTZi6whof2TpSxbvxtqmjVVMZ3VXG77ZfLsxRU0ZateG0235-b4O2NU7p_cKfo5NSVd5cHPoIzR4fZuPnePL69DK-n8SaJmkbE6oJTSDjImGMFgnWmcgUo2AM51yFQnCmcoVxSlPGmWIkzYkSGQ5v65KO0E0fu3bNR2d8K1fWa1NVqjZN52UGBAQXgcAI4V6pXeO9M6VcO7tSbiMxyD1L2bOUgaXcs5Rp8Fwd0rt8ZYo_xy-8ICC9wIdTvTBOLpvO1eHhf1Ove1OpGqkWzno5nxLADAAnLGChP6SHilQ</recordid><startdate>20111001</startdate><enddate>20111001</enddate><creator>Sophiya, K</creator><creator>Anbarasu, Anand</creator><general>Springer-Verlag</general><general>Springer Vienna</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20111001</creationdate><title>Structural stability studies in adhesion molecules—role of cation–π interactions</title><author>Sophiya, K ; Anbarasu, Anand</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c367t-23c23609586443d61c989a430ee555ae55219aba11737454a427b2a891709cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>adhesion</topic><topic>Amino Acid Sequence</topic><topic>Amino Acids - chemistry</topic><topic>arginine</topic><topic>Biomedical and Life Sciences</topic><topic>Cations - chemistry</topic><topic>cell adhesion</topic><topic>Cell Adhesion Molecules - chemistry</topic><topic>Cell Biology</topic><topic>Computational Biology</topic><topic>Conserved Sequence</topic><topic>Databases, Protein</topic><topic>Life Sciences</topic><topic>lysine</topic><topic>Original Article</topic><topic>Plant Sciences</topic><topic>Protein Interaction Mapping</topic><topic>Protein Stability</topic><topic>Protein Structure, Secondary</topic><topic>proteins</topic><topic>Sequence Alignment</topic><topic>Sequence Analysis, Protein</topic><topic>Solvents - chemistry</topic><topic>Zoology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sophiya, K</creatorcontrib><creatorcontrib>Anbarasu, Anand</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Protoplasma</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sophiya, K</au><au>Anbarasu, Anand</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural stability studies in adhesion molecules—role of cation–π interactions</atitle><jtitle>Protoplasma</jtitle><stitle>Protoplasma</stitle><addtitle>Protoplasma</addtitle><date>2011-10-01</date><risdate>2011</risdate><volume>248</volume><issue>4</issue><spage>673</spage><epage>682</epage><pages>673-682</pages><issn>0033-183X</issn><eissn>1615-6102</eissn><abstract>Cell adhesion molecules are important for their various roles in many cellular events and responses. In the present study, we have analyzed the roles played by cation–π interactions in the structural stability of adhesion molecules. These interactions are mainly formed by long-range contacts. The occurrence of arginine is higher than lysine to form cation–π interactions. The secondary structure preferences of interacting residues are independent of amino acid class. Cation–π interactions might stabilize the interface between the terminus and core in this class of proteins. The results obtained in the present study will be useful in understanding the contribution of cation–π interactions to the overall stability of adhesion proteins.</abstract><cop>Vienna</cop><pub>Springer-Verlag</pub><pmid>20978808</pmid><doi>10.1007/s00709-010-0224-7</doi><tpages>10</tpages></addata></record>
fulltext	fulltext
identifier	ISSN: 0033-183X
ispartof	Protoplasma, 2011-10, Vol.248 (4), p.673-682
issn	0033-183X 1615-6102
language	eng
recordid	cdi_proquest_miscellaneous_902085818
source	Springer Nature
subjects	adhesion Amino Acid Sequence Amino Acids - chemistry arginine Biomedical and Life Sciences Cations - chemistry cell adhesion Cell Adhesion Molecules - chemistry Cell Biology Computational Biology Conserved Sequence Databases, Protein Life Sciences lysine Original Article Plant Sciences Protein Interaction Mapping Protein Stability Protein Structure, Secondary proteins Sequence Alignment Sequence Analysis, Protein Solvents - chemistry Zoology
title	Structural stability studies in adhesion molecules—role of cation–π interactions
url	http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T22%3A21%3A46IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structural%20stability%20studies%20in%20adhesion%20molecules%E2%80%94role%20of%20cation%E2%80%93%CF%80%20interactions&rft.jtitle=Protoplasma&rft.au=Sophiya,%20K&rft.date=2011-10-01&rft.volume=248&rft.issue=4&rft.spage=673&rft.epage=682&rft.pages=673-682&rft.issn=0033-183X&rft.eissn=1615-6102&rft_id=info:doi/10.1007/s00709-010-0224-7&rft_dat=%3Cproquest_cross%3E902085818%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c367t-23c23609586443d61c989a430ee555ae55219aba11737454a427b2a891709cf3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=902085818&rft_id=info:pmid/20978808&rfr_iscdi=true