6d21
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the FERM domain of zebrafish FARP2== | |
| + | <StructureSection load='6d21' size='340' side='right' caption='[[6d21]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6d21]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D21 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D21 FirstGlance]. <br> | ||
| + | </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=6d21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d21 OCA], [http://pdbe.org/6d21 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d21 RCSB], [http://www.ebi.ac.uk/pdbsum/6d21 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d21 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | |
| - | [[Category: Kuo, Y | + | <div class="pdbe-citations 6d21" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kuo, Y C]] | ||
[[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 zebrafish FARP2
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