4h6y
From Proteopedia
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| - | + | ==Crystal strucure of the DH-PH-PH domain of FARP1== | |
| - | + | <StructureSection load='4h6y' size='340' side='right' caption='[[4h6y]], [[Resolution|resolution]] 4.09Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4h6y]] is a 2 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=4H6Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H6Y FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gzu|4gzu]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDEP, FARP1, PLEKHC2 ([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=4h6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h6y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h6y RCSB], [http://www.ebi.ac.uk/pdbsum/4h6y PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | FARP2 is a Dbl-family guanine nucleotide exchange factor (GEF) that contains a 4.1, ezrin, radixin and moesin (FERM) domain, a Dbl-homology (DH) domain and two pleckstrin homology (PH) domains. FARP2 activates Rac1 or Cdc42 in response to upstream signals, thereby regulating processes such as neuronal axon guidance and bone homeostasis. How the GEF activity of FARP2 is regulated remained poorly understood. We have determined the crystal structures of the catalytic DH domain and the DH-PH-PH domains of FARP2. The structures reveal an auto-inhibited conformation in which the GEF substrate-binding site is blocked collectively by the last helix in the DH domain and the two PH domains. This conformation is stabilized by multiple interactions among the domains and two well-structured inter-domain linkers. Our cell-based activity assays confirm the suppression of the FARP2 GEF activity by these auto-inhibitory elements. | ||
| - | + | Structural Basis for Autoinhibition of the Guanine Nucleotide Exchange Factor FARP2.,He X, Kuo YC, Rosche TJ, Zhang X Structure. 2013 Mar 5;21(3):355-64. doi: 10.1016/j.str.2013.01.001. Epub 2013 Jan, 31. PMID:23375260<ref>PMID:23375260</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: He, X | + | [[Category: He, X]] |
| - | [[Category: Zhang, X | + | [[Category: Zhang, X]] |
[[Category: Dh-ph]] | [[Category: Dh-ph]] | ||
[[Category: Farp1]] | [[Category: Farp1]] | ||
Revision as of 11:23, 21 December 2014
Crystal strucure of the DH-PH-PH domain of FARP1
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