Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus
•The crystal structure of GKAP homology domain 1 (GH1) was determined.•GKAP GH1 is a three-helix bundle connected by short flexible loops.•The predicted helix α4 associates weakly with the helix α3, suggesting dynamic nature of the GH1 domain. Guanylate-kinase-associated protein (GKAP) is a scaffold...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2014-09, Vol.452 (1), p.130-135 |
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| creator | Tong, Junsen Yang, Huiseon Eom, Soo Hyun Chun, ChangJu Im, Young Jun |
| description | •The crystal structure of GKAP homology domain 1 (GH1) was determined.•GKAP GH1 is a three-helix bundle connected by short flexible loops.•The predicted helix α4 associates weakly with the helix α3, suggesting dynamic nature of the GH1 domain.
Guanylate-kinase-associated protein (GKAP) is a scaffolding protein that links NMDA receptor-PSD-95 to Shank–Homer complexes by protein–protein interactions at the synaptic junction. GKAP family proteins are characterized by the presence of a C-terminal conserved GKAP homology domain 1 (GH1) of unknown structure and function. In this study, crystal structure of the GH1 domain of GKAP from Rattus norvegicus was determined in fusion with an N-terminal maltose-binding protein at 2.0Å resolution. The structure of GKAP GH1 displays a three-helix bundle connected by short flexible loops. The predicted helix α4 which was not visible in the crystal structure associates weakly with the helix α3 suggesting dynamic nature of the GH1 domain. The strict conservation of GH1 domain across GKAP family members and the lack of a catalytic active site required for enzyme activity imply that the GH1 domain might serve as a protein–protein interaction module for the synaptic protein clustering. |
| doi_str_mv | 10.1016/j.bbrc.2014.08.073 |
| format | Article |
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Guanylate-kinase-associated protein (GKAP) is a scaffolding protein that links NMDA receptor-PSD-95 to Shank–Homer complexes by protein–protein interactions at the synaptic junction. GKAP family proteins are characterized by the presence of a C-terminal conserved GKAP homology domain 1 (GH1) of unknown structure and function. In this study, crystal structure of the GH1 domain of GKAP from Rattus norvegicus was determined in fusion with an N-terminal maltose-binding protein at 2.0Å resolution. The structure of GKAP GH1 displays a three-helix bundle connected by short flexible loops. The predicted helix α4 which was not visible in the crystal structure associates weakly with the helix α3 suggesting dynamic nature of the GH1 domain. The strict conservation of GH1 domain across GKAP family members and the lack of a catalytic active site required for enzyme activity imply that the GH1 domain might serve as a protein–protein interaction module for the synaptic protein clustering.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2014.08.073</identifier><identifier>PMID: 25152391</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; Amino Acid Sequence ; Animals ; Calorimetry ; CRYSTAL STRUCTURE ; ENZYME ACTIVITY ; GKAP ; Guanylate Kinases - chemistry ; Helix bundle ; JOINTS ; MALTOSE ; Models, Molecular ; Molecular Sequence Data ; PHOSPHOTRANSFERASES ; Protein Conformation ; PROTEIN STRUCTURE ; Protein Structure, Tertiary ; Protein–protein interaction ; Rats ; RECEPTORS ; RESOLUTION ; Sequence Homology, Amino Acid ; Synaptic scaffolding protein ; X RADIATION ; X-ray crystallography</subject><ispartof>Biochemical and biophysical research communications, 2014-09, Vol.452 (1), p.130-135</ispartof><rights>2014 Elsevier Inc.</rights><rights>Copyright © 2014 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c483t-37255c890ca957128071294c5fa7819a8c749dca219e09d62ef81633290479563</citedby><cites>FETCH-LOGICAL-c483t-37255c890ca957128071294c5fa7819a8c749dca219e09d62ef81633290479563</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2014.08.073$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25152391$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/22416741$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Tong, Junsen</creatorcontrib><creatorcontrib>Yang, Huiseon</creatorcontrib><creatorcontrib>Eom, Soo Hyun</creatorcontrib><creatorcontrib>Chun, ChangJu</creatorcontrib><creatorcontrib>Im, Young Jun</creatorcontrib><title>Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>•The crystal structure of GKAP homology domain 1 (GH1) was determined.•GKAP GH1 is a three-helix bundle connected by short flexible loops.•The predicted helix α4 associates weakly with the helix α3, suggesting dynamic nature of the GH1 domain.
Guanylate-kinase-associated protein (GKAP) is a scaffolding protein that links NMDA receptor-PSD-95 to Shank–Homer complexes by protein–protein interactions at the synaptic junction. GKAP family proteins are characterized by the presence of a C-terminal conserved GKAP homology domain 1 (GH1) of unknown structure and function. In this study, crystal structure of the GH1 domain of GKAP from Rattus norvegicus was determined in fusion with an N-terminal maltose-binding protein at 2.0Å resolution. The structure of GKAP GH1 displays a three-helix bundle connected by short flexible loops. The predicted helix α4 which was not visible in the crystal structure associates weakly with the helix α3 suggesting dynamic nature of the GH1 domain. The strict conservation of GH1 domain across GKAP family members and the lack of a catalytic active site required for enzyme activity imply that the GH1 domain might serve as a protein–protein interaction module for the synaptic protein clustering.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Calorimetry</subject><subject>CRYSTAL STRUCTURE</subject><subject>ENZYME ACTIVITY</subject><subject>GKAP</subject><subject>Guanylate Kinases - chemistry</subject><subject>Helix bundle</subject><subject>JOINTS</subject><subject>MALTOSE</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>PHOSPHOTRANSFERASES</subject><subject>Protein Conformation</subject><subject>PROTEIN STRUCTURE</subject><subject>Protein Structure, Tertiary</subject><subject>Protein–protein interaction</subject><subject>Rats</subject><subject>RECEPTORS</subject><subject>RESOLUTION</subject><subject>Sequence Homology, Amino Acid</subject><subject>Synaptic scaffolding protein</subject><subject>X RADIATION</subject><subject>X-ray crystallography</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEFrFTEQx4Mo9rX6BTzIghcvu53JbrIJeJGirVAo2Ap6CnnZ2TbPt5uaZAv99mZ5rUcvMzD85s-fH2PvEBoElKe7ZruNruGAXQOqgb59wTYIGmqO0L1kGwCQNdf484gdp7QDQOykfs2OuEDBW40b9us6x8XlJVIVxirfUXV-gdUQJuvn9XK72PlxbzNVv_1sE9U2peB8OQzVfQyZCjbGMFXfbc5LquYQH-jWuyW9Ya9Gu0_09mmfsB9fv9ycXdSXV-ffzj5f1q5Tba7bngvhlAZnteiRKyhDd06MtleorXJ9pwdnOWoCPUhOo0LZtlxD12sh2xP24ZAbUvYmOZ_J3bkwz-Sy4bxD2XdYqI8HqpT-s1DKZvLJ0X5vZwpLMigklxJRqILyA-piSCnSaO6jn2x8NAhmFW92ZhVvVvEGlCniy9P7p_xlO9Hw7-XZdAE-HQAqLh48xbUqzY4GH9emQ_D_y_8Lb4GSTg</recordid><startdate>20140912</startdate><enddate>20140912</enddate><creator>Tong, Junsen</creator><creator>Yang, Huiseon</creator><creator>Eom, Soo Hyun</creator><creator>Chun, ChangJu</creator><creator>Im, Young Jun</creator><general>Elsevier Inc</general><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><scope>OTOTI</scope></search><sort><creationdate>20140912</creationdate><title>Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus</title><author>Tong, Junsen ; Yang, Huiseon ; Eom, Soo Hyun ; Chun, ChangJu ; Im, Young Jun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c483t-37255c890ca957128071294c5fa7819a8c749dca219e09d62ef81633290479563</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Calorimetry</topic><topic>CRYSTAL STRUCTURE</topic><topic>ENZYME ACTIVITY</topic><topic>GKAP</topic><topic>Guanylate Kinases - chemistry</topic><topic>Helix bundle</topic><topic>JOINTS</topic><topic>MALTOSE</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>PHOSPHOTRANSFERASES</topic><topic>Protein Conformation</topic><topic>PROTEIN STRUCTURE</topic><topic>Protein Structure, Tertiary</topic><topic>Protein–protein interaction</topic><topic>Rats</topic><topic>RECEPTORS</topic><topic>RESOLUTION</topic><topic>Sequence Homology, Amino Acid</topic><topic>Synaptic scaffolding protein</topic><topic>X RADIATION</topic><topic>X-ray crystallography</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tong, Junsen</creatorcontrib><creatorcontrib>Yang, Huiseon</creatorcontrib><creatorcontrib>Eom, Soo Hyun</creatorcontrib><creatorcontrib>Chun, ChangJu</creatorcontrib><creatorcontrib>Im, Young Jun</creatorcontrib><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><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tong, Junsen</au><au>Yang, Huiseon</au><au>Eom, Soo Hyun</au><au>Chun, ChangJu</au><au>Im, Young Jun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2014-09-12</date><risdate>2014</risdate><volume>452</volume><issue>1</issue><spage>130</spage><epage>135</epage><pages>130-135</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>•The crystal structure of GKAP homology domain 1 (GH1) was determined.•GKAP GH1 is a three-helix bundle connected by short flexible loops.•The predicted helix α4 associates weakly with the helix α3, suggesting dynamic nature of the GH1 domain.
Guanylate-kinase-associated protein (GKAP) is a scaffolding protein that links NMDA receptor-PSD-95 to Shank–Homer complexes by protein–protein interactions at the synaptic junction. GKAP family proteins are characterized by the presence of a C-terminal conserved GKAP homology domain 1 (GH1) of unknown structure and function. In this study, crystal structure of the GH1 domain of GKAP from Rattus norvegicus was determined in fusion with an N-terminal maltose-binding protein at 2.0Å resolution. The structure of GKAP GH1 displays a three-helix bundle connected by short flexible loops. The predicted helix α4 which was not visible in the crystal structure associates weakly with the helix α3 suggesting dynamic nature of the GH1 domain. The strict conservation of GH1 domain across GKAP family members and the lack of a catalytic active site required for enzyme activity imply that the GH1 domain might serve as a protein–protein interaction module for the synaptic protein clustering.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>25152391</pmid><doi>10.1016/j.bbrc.2014.08.073</doi><tpages>6</tpages></addata></record> |
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| subjects | 60 APPLIED LIFE SCIENCES Amino Acid Sequence Animals Calorimetry CRYSTAL STRUCTURE ENZYME ACTIVITY GKAP Guanylate Kinases - chemistry Helix bundle JOINTS MALTOSE Models, Molecular Molecular Sequence Data PHOSPHOTRANSFERASES Protein Conformation PROTEIN STRUCTURE Protein Structure, Tertiary Protein–protein interaction Rats RECEPTORS RESOLUTION Sequence Homology, Amino Acid Synaptic scaffolding protein X RADIATION X-ray crystallography |
| title | Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus |
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