DC Field | Value | Language |
---|---|---|
dc.contributor.author | Im, YJ | ko |
dc.contributor.author | Park, SH | ko |
dc.contributor.author | Rho, SH | ko |
dc.contributor.author | Lee, JH | ko |
dc.contributor.author | Kang, GB | ko |
dc.contributor.author | Sheng, M | ko |
dc.contributor.author | Kim, Eunjoon | ko |
dc.contributor.author | Eom, SH | ko |
dc.date.accessioned | 2013-03-04T03:58:44Z | - |
dc.date.available | 2013-03-04T03:58:44Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2003-03 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.278, pp.8501 - 8507 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10203/81825 | - |
dc.description.abstract | PDZ domains bind to short segments within target proteins in a sequence-specific fashion. Glutamate receptor-interacting protein (GRIP)/ABP family proteins contain six to seven PDZ domains and interact via the sixth PDZ domain (class II) with the C termini of various proteins including liprin-alpha. In addition the PDZ456 domain mediates the formation of homo- and heteromultimers of GRIP proteins. To better understand the structural basis of peptide recognition by a class II PDZ domain and PDZ-mediated multimerization, we determined the crystal structures of the GRIP1 PDZ6 domain alone and in complex with a synthetic C-terminal octapeptide of human liprin-alpha at resolutions of 1.5 and 1.8 Angstrom, respectively. Remarkably, unlike other class II PDZ domains, Ile-736 at alphaB5 rather than conserved Leu-732 at alphaB1 makes a direct hydrophobic contact with the side chain of the Tyr at the -2 position of the ligand. Moreover, the peptide-bound structure of PDZ6 shows a slight reorientation of helix all, indicating that the second hydrophobic pocket undergoes a conformational adaptation to accommodate the bulkiness of the Tyr side chain, and forms an antiparallel dimer through an interface located at a site distal to the peptide-binding groove. This configuration may enable formation of GRIP multimers and efficient clustering of GRIP-binding proteins. | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | PROTEIN-TYROSINE-PHOSPHATASE | - |
dc.subject | INTERACTING PROTEINS | - |
dc.subject | ADAPTER PROTEINS | - |
dc.subject | AMPA RECEPTORS | - |
dc.subject | ASSOCIATION | - |
dc.subject | DENSITY | - |
dc.subject | MECHANISM | - |
dc.subject | LIGANDS | - |
dc.subject | FAMILY | - |
dc.subject | INAD | - |
dc.title | Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class IIPDZ target recognition and PDZ domain-mediated multimerization | - |
dc.type | Article | - |
dc.identifier.wosid | 000181466800098 | - |
dc.identifier.scopusid | 2-s2.0-0037424515 | - |
dc.type.rims | ART | - |
dc.citation.volume | 278 | - |
dc.citation.beginningpage | 8501 | - |
dc.citation.endingpage | 8507 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.contributor.localauthor | Kim, Eunjoon | - |
dc.contributor.nonIdAuthor | Im, YJ | - |
dc.contributor.nonIdAuthor | Park, SH | - |
dc.contributor.nonIdAuthor | Rho, SH | - |
dc.contributor.nonIdAuthor | Lee, JH | - |
dc.contributor.nonIdAuthor | Kang, GB | - |
dc.contributor.nonIdAuthor | Sheng, M | - |
dc.contributor.nonIdAuthor | Eom, SH | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | PROTEIN-TYROSINE-PHOSPHATASE | - |
dc.subject.keywordPlus | INTERACTING PROTEINS | - |
dc.subject.keywordPlus | ADAPTER PROTEINS | - |
dc.subject.keywordPlus | AMPA RECEPTORS | - |
dc.subject.keywordPlus | ASSOCIATION | - |
dc.subject.keywordPlus | DENSITY | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | LIGANDS | - |
dc.subject.keywordPlus | FAMILY | - |
dc.subject.keywordPlus | INAD | - |
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