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| | <StructureSection load='6d2q' size='340' side='right'caption='[[6d2q]], [[Resolution|resolution]] 2.99Å' scene=''> | | <StructureSection load='6d2q' size='340' side='right'caption='[[6d2q]], [[Resolution|resolution]] 2.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6d2q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D2Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6d2q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D2Q FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6d21|6d21]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.99Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">farp1, si:ch211-235f1.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6d2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d2q OCA], [https://pdbe.org/6d2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d2q RCSB], [https://www.ebi.ac.uk/pdbsum/6d2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d2q ProSAT]</span></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=6d2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d2q OCA], [http://pdbe.org/6d2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d2q RCSB], [http://www.ebi.ac.uk/pdbsum/6d2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d2q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E9QIC8_DANRE E9QIC8_DANRE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Brachidanio rerio]] | + | [[Category: Danio rerio]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kuo, Y C]] | + | [[Category: Kuo YC]] |
| - | [[Category: Zhang, X]] | + | [[Category: Zhang X]] |
| - | [[Category: Membrane targeting]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
E9QIC8_DANRE
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kuo YC, He X, Coleman AJ, Chen YJ, Dasari P, Liou J, Biederer T, Zhang X. Structural analyses of FERM domain-mediated membrane localization of FARP1. Sci Rep. 2018 Jul 11;8(1):10477. doi: 10.1038/s41598-018-28692-4. PMID:29992992 doi:http://dx.doi.org/10.1038/s41598-018-28692-4
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