6d21

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:32, 13 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='6d21' size='340' side='right'caption='[[6d21]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='6d21' size='340' side='right'caption='[[6d21]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6d21]] 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=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>
+
<table><tr><td colspan='2'>[[6d21]] 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=6D21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D21 FirstGlance]. <br>
-
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">farp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</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]] 1.999&#8491;</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>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6d21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d21 OCA], [https://pdbe.org/6d21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d21 RCSB], [https://www.ebi.ac.uk/pdbsum/6d21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d21 ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/E7FE33_DANRE E7FE33_DANRE]
-
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 6d21" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__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]]
+

Current revision

Crystal structure of the FERM domain of zebrafish FARP2

PDB ID 6d21

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools