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Crystal structure of a PDZ domain
PDZ domains (also known as DHR domains or GLGF repeats) are ~90-residue repeats found in a number of proteins implicated in ion-channel and receptor clustering, and the linking of receptors to effector enzymes1. PDZ domains are protein-recognition modules; some recognize proteins containing the cons...
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| Published in: | Nature (London) 1996-08, Vol.382 (6592), p.649-652 |
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| Main Authors: | , , , , , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c386t-ddd1be28ae02489fc02168d3485c891dd6949ca62867b23e4f42364ef095b01c3 |
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| cites | cdi_FETCH-LOGICAL-c386t-ddd1be28ae02489fc02168d3485c891dd6949ca62867b23e4f42364ef095b01c3 |
| container_end_page | 652 |
| container_issue | 6592 |
| container_start_page | 649 |
| container_title | Nature (London) |
| container_volume | 382 |
| creator | Cabral, João H. Morais Petosa, Carlo Sutcliffe, Michael J Raza, Sami Byron, Olwyn Poy, Florence Marfatia, Shirin M Chishti, Athar H Liddington, Robert C |
| description | PDZ domains (also known as DHR domains or GLGF repeats) are ~90-residue repeats found in a number of proteins implicated in ion-channel and receptor clustering, and the linking of receptors to effector enzymes1. PDZ domains are protein-recognition modules; some recognize proteins containing the consensus carboxy-terminal tripeptide motif S/TXV with high specificity
2–4
. Other PDZ domains form homotypic dimers: the PDZ domain of the neuronal enzyme nitric oxide synthase binds to the PDZ domain of PSD-95, an interaction that has been implicated in its synaptic association
5
. Here we report the crystal structure of the third PDZ domain of the human homologue of the
Drosophila discs-large
tumour-suppressor gene product, DlgA. It consists of a five-stranded antiparallel β-barrel flanked by three α-helices. A groove runs over the surface of the domain, ending in a conserved hydrophobic pocket and a buried arginine; we suggest that this is the binding site for the C-terminal peptide. |
| doi_str_mv | 10.1038/382649a0 |
| format | article |
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2–4
. Other PDZ domains form homotypic dimers: the PDZ domain of the neuronal enzyme nitric oxide synthase binds to the PDZ domain of PSD-95, an interaction that has been implicated in its synaptic association
5
. Here we report the crystal structure of the third PDZ domain of the human homologue of the
Drosophila discs-large
tumour-suppressor gene product, DlgA. It consists of a five-stranded antiparallel β-barrel flanked by three α-helices. A groove runs over the surface of the domain, ending in a conserved hydrophobic pocket and a buried arginine; we suggest that this is the binding site for the C-terminal peptide.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/382649a0</identifier><identifier>PMID: 8757139</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Binding and carrier proteins ; Binding Sites ; Biochemistry ; Biological and medical sciences ; Crystallography, X-Ray ; Crystals ; Drosophila ; Fundamental and applied biological sciences. Psychology ; Genes ; Genes, Tumor Suppressor ; Humanities and Social Sciences ; Humans ; Ions ; letter ; Membrane Proteins ; Models, Molecular ; Molecular Sequence Data ; multidisciplinary ; Nitric oxide ; Proteins ; Proteins - chemistry ; Proteins - genetics ; Recombinant Proteins - chemistry ; Science ; Science (multidisciplinary) ; Sequence Homology, Amino Acid</subject><ispartof>Nature (London), 1996-08, Vol.382 (6592), p.649-652</ispartof><rights>Springer Nature Limited 1996</rights><rights>1996 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Aug 15, 1996</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-ddd1be28ae02489fc02168d3485c891dd6949ca62867b23e4f42364ef095b01c3</citedby><cites>FETCH-LOGICAL-c386t-ddd1be28ae02489fc02168d3485c891dd6949ca62867b23e4f42364ef095b01c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3169008$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8757139$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cabral, João H. Morais</creatorcontrib><creatorcontrib>Petosa, Carlo</creatorcontrib><creatorcontrib>Sutcliffe, Michael J</creatorcontrib><creatorcontrib>Raza, Sami</creatorcontrib><creatorcontrib>Byron, Olwyn</creatorcontrib><creatorcontrib>Poy, Florence</creatorcontrib><creatorcontrib>Marfatia, Shirin M</creatorcontrib><creatorcontrib>Chishti, Athar H</creatorcontrib><creatorcontrib>Liddington, Robert C</creatorcontrib><title>Crystal structure of a PDZ domain</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>PDZ domains (also known as DHR domains or GLGF repeats) are ~90-residue repeats found in a number of proteins implicated in ion-channel and receptor clustering, and the linking of receptors to effector enzymes1. PDZ domains are protein-recognition modules; some recognize proteins containing the consensus carboxy-terminal tripeptide motif S/TXV with high specificity
2–4
. Other PDZ domains form homotypic dimers: the PDZ domain of the neuronal enzyme nitric oxide synthase binds to the PDZ domain of PSD-95, an interaction that has been implicated in its synaptic association
5
. Here we report the crystal structure of the third PDZ domain of the human homologue of the
Drosophila discs-large
tumour-suppressor gene product, DlgA. It consists of a five-stranded antiparallel β-barrel flanked by three α-helices. A groove runs over the surface of the domain, ending in a conserved hydrophobic pocket and a buried arginine; we suggest that this is the binding site for the C-terminal peptide.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding and carrier proteins</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>Drosophila</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes</subject><subject>Genes, Tumor Suppressor</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Ions</subject><subject>letter</subject><subject>Membrane Proteins</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>multidisciplinary</subject><subject>Nitric oxide</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><subject>Recombinant Proteins - chemistry</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Sequence Homology, Amino Acid</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNqF0ctKxDAUBuAgyjiOgi-gVBEvi-rJpbksZbzCgC5046akaSodOu2YtIt5ezPMDUR0lcX5-HOSH6FDDNcYqLyhknCmNGyhPmaCx4xLsY36AETGICnfRXvejwEgwYL1UE-KRGCq-uhk6Ga-1VXkW9eZtnM2aopIR693H1HeTHRZ76OdQlfeHizPAXp_uH8bPsWjl8fn4e0oNlTyNs7zHGeWSG2BMKkKAwRzmVMmEyMVznOumDKaE8lFRqhlBSOUM1uASjLAhg7Q-SJ36pqvzvo2nZTe2KrStW06nwoZfIJVgBd_Q0ZxQkCqfyNxwsOOQgR4-gOOm87V4bkpAcY4pYIGdLlAxjXeO1ukU1dOtJulGNJ5C-mqhUCPlnldNrH5Gi6_PczPlnPtja4Kp2tT-jWjmCsItQ3Q1YL5MKk_rdus9cuVxwtb63mLm6wV-AYqNKEl</recordid><startdate>19960815</startdate><enddate>19960815</enddate><creator>Cabral, João H. 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cabral, João H. Morais</au><au>Petosa, Carlo</au><au>Sutcliffe, Michael J</au><au>Raza, Sami</au><au>Byron, Olwyn</au><au>Poy, Florence</au><au>Marfatia, Shirin M</au><au>Chishti, Athar H</au><au>Liddington, Robert C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of a PDZ domain</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1996-08-15</date><risdate>1996</risdate><volume>382</volume><issue>6592</issue><spage>649</spage><epage>652</epage><pages>649-652</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>PDZ domains (also known as DHR domains or GLGF repeats) are ~90-residue repeats found in a number of proteins implicated in ion-channel and receptor clustering, and the linking of receptors to effector enzymes1. PDZ domains are protein-recognition modules; some recognize proteins containing the consensus carboxy-terminal tripeptide motif S/TXV with high specificity
2–4
. Other PDZ domains form homotypic dimers: the PDZ domain of the neuronal enzyme nitric oxide synthase binds to the PDZ domain of PSD-95, an interaction that has been implicated in its synaptic association
5
. Here we report the crystal structure of the third PDZ domain of the human homologue of the
Drosophila discs-large
tumour-suppressor gene product, DlgA. It consists of a five-stranded antiparallel β-barrel flanked by three α-helices. A groove runs over the surface of the domain, ending in a conserved hydrophobic pocket and a buried arginine; we suggest that this is the binding site for the C-terminal peptide.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>8757139</pmid><doi>10.1038/382649a0</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1996-08, Vol.382 (6592), p.649-652 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78236519 |
| source | Nature |
| subjects | Adaptor Proteins, Signal Transducing Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Binding and carrier proteins Binding Sites Biochemistry Biological and medical sciences Crystallography, X-Ray Crystals Drosophila Fundamental and applied biological sciences. Psychology Genes Genes, Tumor Suppressor Humanities and Social Sciences Humans Ions letter Membrane Proteins Models, Molecular Molecular Sequence Data multidisciplinary Nitric oxide Proteins Proteins - chemistry Proteins - genetics Recombinant Proteins - chemistry Science Science (multidisciplinary) Sequence Homology, Amino Acid |
| title | Crystal structure of a PDZ domain |
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