DC Field | Value | Language |
---|---|---|
dc.contributor.author | Im, YJ | ko |
dc.contributor.author | Lee, JH | ko |
dc.contributor.author | Park, SH | ko |
dc.contributor.author | Park, SJ | ko |
dc.contributor.author | Rho, SH | ko |
dc.contributor.author | Kang, GB | ko |
dc.contributor.author | Kim, Eunjoon | ko |
dc.contributor.author | Eom, SH | ko |
dc.date.accessioned | 2013-03-04T08:00:49Z | - |
dc.date.available | 2013-03-04T08:00:49Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2003-11 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.278, no.48, pp.48099 - 48104 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10203/82089 | - |
dc.description.abstract | The Shank/proline-rich synapse-associated protein family of multidomain proteins is known to play an important role in the organization of synaptic multiprotein complexes. For instance, the Shank PDZ domain binds to the C termini of guanylate kinase-associated proteins, which in turn interact with the guanylate kinase domain of postsynaptic density-95 scaffolding proteins. Here we describe the crystal structures of Shank1 PDZ in its peptide free form and in complex with the C-terminal hexapeptide (EAQTRL) of guanylate kinase-associated protein (GKAP1a) determined at 1.8- and 2.25-Angstrom resolutions, respectively. The structure shows the typical class I PDZ interaction of PDZ-peptide complex with the consensus sequence -X-(Thr/Ser)-X-Leu. In addition, Asp-634 within the Shank1 PDZ domain recognizes the positively charged Arg at - 1 position and hydrogen bonds, and salt bridges between Arg-607 and the side chains of the ligand at - 3 and - 5 positions contribute further to the recognition of the peptide ligand. Remarkably, whether free or complexed, Shank1 PDZ domains form dimers with a conserved betaB/betaC loop and N-terminal betaA strands, suggesting a novel model of PDZ-PDZ homodimerization. This implies that antiparallel dimerization through the N-terminal betaA strands could be a common configuration among PDZ dimers. Within the dimeric structure, the two-peptide binding sites are arranged so that the N termini of the bound peptide ligands are in close proximity and oriented toward the 2-fold axis of the dimer. This configuration may provide a means of facilitating dimeric organization of PDZ-target assemblies. | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | POSTSYNAPTIC DENSITY PROTEINS | - |
dc.subject | SYNAPTIC PROTEINS | - |
dc.subject | CARBOXYL-TERMINI | - |
dc.subject | BETA-PIX | - |
dc.subject | FAMILY | - |
dc.subject | DOMAIN | - |
dc.subject | RECOGNITION | - |
dc.subject | MULTIMERIZATION | - |
dc.subject | ASSOCIATION | - |
dc.subject | REGULATOR | - |
dc.title | Crystal structure of the Shank PDZ-ligand complex reveals a class IPDZ interaction and a novel PDZ-PDZ dimerization | - |
dc.type | Article | - |
dc.identifier.wosid | 000186731400090 | - |
dc.identifier.scopusid | 2-s2.0-0348111461 | - |
dc.type.rims | ART | - |
dc.citation.volume | 278 | - |
dc.citation.issue | 48 | - |
dc.citation.beginningpage | 48099 | - |
dc.citation.endingpage | 48104 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.contributor.localauthor | Kim, Eunjoon | - |
dc.contributor.nonIdAuthor | Im, YJ | - |
dc.contributor.nonIdAuthor | Lee, JH | - |
dc.contributor.nonIdAuthor | Park, SH | - |
dc.contributor.nonIdAuthor | Park, SJ | - |
dc.contributor.nonIdAuthor | Rho, SH | - |
dc.contributor.nonIdAuthor | Kang, GB | - |
dc.contributor.nonIdAuthor | Eom, SH | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | POSTSYNAPTIC DENSITY PROTEINS | - |
dc.subject.keywordPlus | SYNAPTIC PROTEINS | - |
dc.subject.keywordPlus | CARBOXYL-TERMINI | - |
dc.subject.keywordPlus | BETA-PIX | - |
dc.subject.keywordPlus | FAMILY | - |
dc.subject.keywordPlus | DOMAIN | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | MULTIMERIZATION | - |
dc.subject.keywordPlus | ASSOCIATION | - |
dc.subject.keywordPlus | REGULATOR | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.