3w9y
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of the human DLG1 guanylate kinase domain== | |
| - | + | <StructureSection load='3w9y' size='340' side='right' caption='[[3w9y]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3w9y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W9Y FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DLG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w9y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w9y RCSB], [http://www.ebi.ac.uk/pdbsum/3w9y PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/DLG1_HUMAN DLG1_HUMAN]] Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel.<ref>PMID:10656683</ref> <ref>PMID:12445884</ref> <ref>PMID:14699157</ref> <ref>PMID:15263016</ref> <ref>PMID:19213956</ref> <ref>PMID:20605917</ref> | [[http://www.uniprot.org/uniprot/DLG1_HUMAN DLG1_HUMAN]] Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel.<ref>PMID:10656683</ref> <ref>PMID:12445884</ref> <ref>PMID:14699157</ref> <ref>PMID:15263016</ref> <ref>PMID:19213956</ref> <ref>PMID:20605917</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Discs large homolog 1 (DLG1/SAP97) is involved in the development and regulation of neuronal and immunological synapses. DLG1 is a member of the membrane associated guanylate kinase (MAGUK) family of proteins, which function as molecular scaffolds. The C-terminal guanylate kinase (GK) domain of DLG1 binds peptides with a phosphorylated serine residue. In this study, we solved the crystal structure of the GK domain of human DLG1. The C-terminal tail of DLG1 is bound to the peptide-binding site of an adjacent symmetry-related DLG1 GK molecule. The binding direction of the C-terminal tail to the peptide-binding site is opposite to that of the phosphorylated LGN peptide in complex with the rat DLG1 GK domain. The C-terminal tail forms a 310 helix, which is also different from the conformation of the phosphorylated LGN peptide. Nevertheless, the side chain interactions of the C-terminal tail with the DLG1 GK domain are similar to those of the phosphorylated LGN peptide. | ||
| - | + | Crystal structure of the guanylate kinase domain from discs large homolog 1 (DLG1/SAP97).,Mori S, Tezuka Y, Arakawa A, Handa N, Shirouzu M, Akiyama T, Yokoyama S Biochem Biophys Res Commun. 2013 Jun 7;435(3):334-8. doi:, 10.1016/j.bbrc.2013.04.056. Epub 2013 Apr 25. PMID:23624197<ref>PMID:23624197</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Akiyama, T | + | [[Category: Akiyama, T]] |
| - | [[Category: Arakawa, A | + | [[Category: Arakawa, A]] |
| - | [[Category: Handa, N | + | [[Category: Handa, N]] |
| - | [[Category: Mori, S | + | [[Category: Mori, S]] |
| - | [[Category: Shirouzu, M | + | [[Category: Shirouzu, M]] |
| - | [[Category: Tezuka, Y | + | [[Category: Tezuka, Y]] |
| - | [[Category: Yokoyama, S | + | [[Category: Yokoyama, S]] |
[[Category: Cell membrane]] | [[Category: Cell membrane]] | ||
[[Category: Guanylate kinase]] | [[Category: Guanylate kinase]] | ||
Revision as of 01:04, 25 December 2014
Crystal structure of the human DLG1 guanylate kinase domain
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