6d2k
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the FERM domain of mouse FARP2== | |
| + | <StructureSection load='6d2k' size='340' side='right' caption='[[6d2k]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6d2k]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D2K FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6d21|6d21]]</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=6d2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d2k OCA], [http://pdbe.org/6d2k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d2k RCSB], [http://www.ebi.ac.uk/pdbsum/6d2k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d2k ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FARP2_MOUSE FARP2_MOUSE]] Rho-guanine nucleotide exchange factor that activates RAC1. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton.<ref>PMID:12351724</ref> <ref>PMID:16286926</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | FARP1 is a multi-domain protein that is involved in regulating neuronal development through interacting with cell surface proteins such as class A Plexins and SynCAM 1. The N-terminal FERM domain in FARP1 is known to both promote membrane localization and mediate these protein interactions, for which the underlying molecular mechanisms remain unclear. Here we determined the crystal structures of the FERM domain of FARP1 from zebrafish, and those of FARP2 (a close homolog of FARP1) from mouse and zebrafish. These FERM domains adopt the three-leaved clover fold that is typical of all FERM domains. Our structures reveal a positively charged surface patch that is highly conserved in the FERM domain of FARP1 and FARP2. In vitro lipid-binding experiments showed that the FARP1 FERM domain binds specifically to several types of phospholipid, which is dependent on the positively charged surface patch. We further determined through cell-based analyses that this surface patch on the FERM domain underlies the localization of FARP1 to the plasma membrane, and that FERM domain interactions recruit it to postsynaptic sites in neurons. | ||
| - | + | Structural analyses of FERM domain-mediated membrane localization of FARP1.,Kuo YC, He X, Coleman AJ, Chen YJ, Dasari P, Liou J, Biederer T, Zhang X Sci Rep. 2018 Jul 11;8(1):10477. doi: 10.1038/s41598-018-28692-4. PMID:29992992<ref>PMID:29992992</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 6d2k" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: He, X]] | [[Category: He, X]] | ||
[[Category: Zhang, X]] | [[Category: Zhang, X]] | ||
| + | [[Category: Membrane targeting]] | ||
| + | [[Category: Signaling protein]] | ||
Revision as of 07:36, 18 July 2018
Crystal structure of the FERM domain of mouse FARP2
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