Structural Basis for the Molecular Recognition between Human Splicing Factors U2AF and SF1/mBBP

The essential splicing factors SF1 and U2AF play an important role in the recognition of the pre-mRNA 3' splice site during early spliceosome assembly. The structure of the C-terminal RRM (RRM3) of human U2AF super(65) complexed to an N-terminal peptide of SF1 reveals an extended negatively cha...

Full description

Saved in:
Bibliographic Details
Published in:Molecular cell 2003-04, Vol.11 (4), p.965-976
Main Authors: Selenko, P, Gregorovic, G, Sprangers, R, Stier, G, Rhani, Z, Kraemer, A, Sattler, M
Format: Article
Language:English
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page 976
container_issue 4
container_start_page 965
container_title Molecular cell
container_volume 11
creator Selenko, P
Gregorovic, G
Sprangers, R
Stier, G
Rhani, Z
Kraemer, A
Sattler, M
description The essential splicing factors SF1 and U2AF play an important role in the recognition of the pre-mRNA 3' splice site during early spliceosome assembly. The structure of the C-terminal RRM (RRM3) of human U2AF super(65) complexed to an N-terminal peptide of SF1 reveals an extended negatively charged helix A and an additional helix C. Helix C shields the potential RNA binding surface. SF1 binds to the opposite, helical face of RRM3. It inserts a conserved tryptophan into a hydrophobic pocket between helices A and B in a way that strikingly resembles part of the molecular interface in the U2AF heterodimer. This molecular recognition establishes a paradigm for protein binding by a subfamily of noncanonical RRMs.
doi_str_mv 10.1016/S1097-2765(03)00115-1
format article
fullrecord <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_miscellaneous_18737499</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>18737499</sourcerecordid><originalsourceid>FETCH-LOGICAL-p184t-f674c2befffe5542d849bf6f8ceae2468a12d27afcb57ae25ac59ea8632dc7ff3</originalsourceid><addsrcrecordid>eNo9jEFLwzAYQHNQcE5_gpCT6KGuSZMmPW7DOmGiWHceX9Mvs5Ils0nZ33egeHrwHjxCblj-wHJWzhqWVyrjqpR3eXGf54zJjJ2Ryb--IJcxfp2CkLqakG2ThtGkcQBHFxD7SG0YaPpE-hIcmtHBQN_RhJ3vUx88bTEdET1djXvwtDm43vR-R2swKQyRbvi8puA72tRstl8s3q7IuQUX8fqPU7KpHz-Wq2z9-vS8nK-zA9MiZbZUwvAWrbUopeCdFlVrS6sNAnJRamC84wqsaaU6GQlGVgi6LHhnlLXFlNz-fg9D-B4xpu2-jwadA49hjFumVaFEVRU_yoBXXA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18737499</pqid></control><display><type>article</type><title>Structural Basis for the Molecular Recognition between Human Splicing Factors U2AF and SF1/mBBP</title><source>BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS</source><creator>Selenko, P ; Gregorovic, G ; Sprangers, R ; Stier, G ; Rhani, Z ; Kraemer, A ; Sattler, M</creator><creatorcontrib>Selenko, P ; Gregorovic, G ; Sprangers, R ; Stier, G ; Rhani, Z ; Kraemer, A ; Sattler, M</creatorcontrib><description>The essential splicing factors SF1 and U2AF play an important role in the recognition of the pre-mRNA 3' splice site during early spliceosome assembly. The structure of the C-terminal RRM (RRM3) of human U2AF super(65) complexed to an N-terminal peptide of SF1 reveals an extended negatively charged helix A and an additional helix C. Helix C shields the potential RNA binding surface. SF1 binds to the opposite, helical face of RRM3. It inserts a conserved tryptophan into a hydrophobic pocket between helices A and B in a way that strikingly resembles part of the molecular interface in the U2AF heterodimer. This molecular recognition establishes a paradigm for protein binding by a subfamily of noncanonical RRMs.</description><identifier>ISSN: 1097-2765</identifier><identifier>DOI: 10.1016/S1097-2765(03)00115-1</identifier><language>eng</language><ispartof>Molecular cell, 2003-04, Vol.11 (4), p.965-976</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></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></links><search><creatorcontrib>Selenko, P</creatorcontrib><creatorcontrib>Gregorovic, G</creatorcontrib><creatorcontrib>Sprangers, R</creatorcontrib><creatorcontrib>Stier, G</creatorcontrib><creatorcontrib>Rhani, Z</creatorcontrib><creatorcontrib>Kraemer, A</creatorcontrib><creatorcontrib>Sattler, M</creatorcontrib><title>Structural Basis for the Molecular Recognition between Human Splicing Factors U2AF and SF1/mBBP</title><title>Molecular cell</title><description>The essential splicing factors SF1 and U2AF play an important role in the recognition of the pre-mRNA 3' splice site during early spliceosome assembly. The structure of the C-terminal RRM (RRM3) of human U2AF super(65) complexed to an N-terminal peptide of SF1 reveals an extended negatively charged helix A and an additional helix C. Helix C shields the potential RNA binding surface. SF1 binds to the opposite, helical face of RRM3. It inserts a conserved tryptophan into a hydrophobic pocket between helices A and B in a way that strikingly resembles part of the molecular interface in the U2AF heterodimer. This molecular recognition establishes a paradigm for protein binding by a subfamily of noncanonical RRMs.</description><issn>1097-2765</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNo9jEFLwzAYQHNQcE5_gpCT6KGuSZMmPW7DOmGiWHceX9Mvs5Ils0nZ33egeHrwHjxCblj-wHJWzhqWVyrjqpR3eXGf54zJjJ2Ryb--IJcxfp2CkLqakG2ThtGkcQBHFxD7SG0YaPpE-hIcmtHBQN_RhJ3vUx88bTEdET1djXvwtDm43vR-R2swKQyRbvi8puA72tRstl8s3q7IuQUX8fqPU7KpHz-Wq2z9-vS8nK-zA9MiZbZUwvAWrbUopeCdFlVrS6sNAnJRamC84wqsaaU6GQlGVgi6LHhnlLXFlNz-fg9D-B4xpu2-jwadA49hjFumVaFEVRU_yoBXXA</recordid><startdate>20030401</startdate><enddate>20030401</enddate><creator>Selenko, P</creator><creator>Gregorovic, G</creator><creator>Sprangers, R</creator><creator>Stier, G</creator><creator>Rhani, Z</creator><creator>Kraemer, A</creator><creator>Sattler, M</creator><scope>7TM</scope></search><sort><creationdate>20030401</creationdate><title>Structural Basis for the Molecular Recognition between Human Splicing Factors U2AF and SF1/mBBP</title><author>Selenko, P ; Gregorovic, G ; Sprangers, R ; Stier, G ; Rhani, Z ; Kraemer, A ; Sattler, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p184t-f674c2befffe5542d849bf6f8ceae2468a12d27afcb57ae25ac59ea8632dc7ff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Selenko, P</creatorcontrib><creatorcontrib>Gregorovic, G</creatorcontrib><creatorcontrib>Sprangers, R</creatorcontrib><creatorcontrib>Stier, G</creatorcontrib><creatorcontrib>Rhani, Z</creatorcontrib><creatorcontrib>Kraemer, A</creatorcontrib><creatorcontrib>Sattler, M</creatorcontrib><collection>Nucleic Acids Abstracts</collection><jtitle>Molecular cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Selenko, P</au><au>Gregorovic, G</au><au>Sprangers, R</au><au>Stier, G</au><au>Rhani, Z</au><au>Kraemer, A</au><au>Sattler, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Basis for the Molecular Recognition between Human Splicing Factors U2AF and SF1/mBBP</atitle><jtitle>Molecular cell</jtitle><date>2003-04-01</date><risdate>2003</risdate><volume>11</volume><issue>4</issue><spage>965</spage><epage>976</epage><pages>965-976</pages><issn>1097-2765</issn><abstract>The essential splicing factors SF1 and U2AF play an important role in the recognition of the pre-mRNA 3' splice site during early spliceosome assembly. The structure of the C-terminal RRM (RRM3) of human U2AF super(65) complexed to an N-terminal peptide of SF1 reveals an extended negatively charged helix A and an additional helix C. Helix C shields the potential RNA binding surface. SF1 binds to the opposite, helical face of RRM3. It inserts a conserved tryptophan into a hydrophobic pocket between helices A and B in a way that strikingly resembles part of the molecular interface in the U2AF heterodimer. This molecular recognition establishes a paradigm for protein binding by a subfamily of noncanonical RRMs.</abstract><doi>10.1016/S1097-2765(03)00115-1</doi><tpages>12</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1097-2765
ispartof Molecular cell, 2003-04, Vol.11 (4), p.965-976
issn 1097-2765
language eng
recordid cdi_proquest_miscellaneous_18737499
source BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS
title Structural Basis for the Molecular Recognition between Human Splicing Factors U2AF and SF1/mBBP
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T18%3A07%3A05IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structural%20Basis%20for%20the%20Molecular%20Recognition%20between%20Human%20Splicing%20Factors%20U2AF%20and%20SF1/mBBP&rft.jtitle=Molecular%20cell&rft.au=Selenko,%20P&rft.date=2003-04-01&rft.volume=11&rft.issue=4&rft.spage=965&rft.epage=976&rft.pages=965-976&rft.issn=1097-2765&rft_id=info:doi/10.1016/S1097-2765(03)00115-1&rft_dat=%3Cproquest%3E18737499%3C/proquest%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-p184t-f674c2befffe5542d849bf6f8ceae2468a12d27afcb57ae25ac59ea8632dc7ff3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=18737499&rft_id=info:pmid/&rfr_iscdi=true