View source for 6f55


==Complex structure of PACSIN SH3 domain and TRPV4 proline rich region==
<StructureSection load='6f55' size='340' side='right'caption='[[6f55]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6f55]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F55 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PACSIN3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=6f55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f55 OCA], [http://pdbe.org/6f55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f55 RCSB], [http://www.ebi.ac.uk/pdbsum/6f55 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f55 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Transient receptor potential (TRP) channels are polymodally regulated ion channels. TRPV4 (vanilloid 4) is sensitized by PIP2 and desensitized by Syndapin3/PACSIN3, which bind to the structurally uncharacterized TRPV4 N terminus. We determined the nuclear magnetic resonance structure of the Syndapin3/PACSIN3 SH3 domain in complex with the TRPV4 N-terminal proline-rich region (PRR), which binds as a class I polyproline II (PPII) helix. This PPII conformation is broken by a conserved proline in a cis conformation. Beyond the PPII, we find that the proximal TRPV4 N terminus is unstructured, a feature conserved across species thus explaining the difficulties in resolving it in previous structural studies. Syndapin/PACSIN SH3 domain binding leads to rigidification of both the PRR and the adjacent PIP2 binding site. We determined the affinities of the TRPV4 N terminus for PACSIN1, 2, and 3 SH3 domains and PIP2 and deduce a hierarchical interaction network where Syndapin/PACSIN binding influences the PIP2 binding site but not vice versa.

Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP2.,Goretzki B, Glogowski NA, Diehl E, Duchardt-Ferner E, Hacker C, Gaudet R, Hellmich UA Structure. 2018 Aug 14. pii: S0969-2126(18)30290-9. doi:, 10.1016/j.str.2018.08.002. PMID:30244966<ref>PMID:30244966</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6f55" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chick]]
[[Category: Large Structures]]
[[Category: Diehl, E]]
[[Category: Duchardt-Ferner, E]]
[[Category: Glogowski, N A]]
[[Category: Goretzki, B]]
[[Category: Hacker, C]]
[[Category: Hellmich, U A]]
[[Category: Peptide binding protein]]
[[Category: Protein]]