4n5q: Difference between revisions
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==Crystal structure of the N-terminal ankyrin repeat domain of TRPV3== | |||
<StructureSection load='4n5q' size='340' side='right' caption='[[4n5q]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4n5q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N5Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N5Q FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Trpv3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4n5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n5q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n5q RCSB], [http://www.ebi.ac.uk/pdbsum/4n5q PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In all six members of TRPV channel subfamily, there is an ankyrin repeat domain (ARD) in their intracellular N-termini. Ankyrin (ANK) repeat, a common motif with typically 33 residues in each repeat, is primarily involved in protein-protein interactions. Despite the sequence similarity among the ARDs of TRPV channels, the structure of TRPV3-ARD, however, remains unknown. Here, we report the crystal structure of TRPV3-ARD solved at 1.95 A resolution, which reveals six-ankyrin repeats. While overall structure of TRPV3-ARD is similar to ARDs from other members of TRPV subfamily; it, however, features a noticeable finger 3 loop that bends over and is stabilized by a network of hydrogen bonds and hydrophobic packing, instead of being flexible as seen in known TRPV-ARD structures. Electrophysiological recordings demonstrated that mutating key residues R225, R226, Q255, and F249 of finger 3 loop altered the channel activities and pharmacology. Taken all together, our findings show that TRPV3-ARD with characteristic finger 3 loop likely plays an important role in channel function and pharmacology. | |||
Crystal structure of the N-terminal ankyrin repeat domain of TRPV3 reveals unique conformation of finger 3 loop critical for channel function.,Shi DJ, Ye S, Cao X, Zhang R, Wang K Protein Cell. 2013 Dec;4(12):942-50. doi: 10.1007/s13238-013-3091-0. Epub 2013, Nov 18. PMID:24248473<ref>PMID:24248473</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
[[Category: Cao, X | </StructureSection> | ||
[[Category: Shi, D J | [[Category: Lk3 transgenic mice]] | ||
[[Category: Wang, K W | [[Category: Cao, X]] | ||
[[Category: Ye, S | [[Category: Shi, D J]] | ||
[[Category: Zhang, R | [[Category: Wang, K W]] | ||
[[Category: Ye, S]] | |||
[[Category: Zhang, R]] | |||
[[Category: Ankyrin]] | [[Category: Ankyrin]] | ||
[[Category: Channel]] | [[Category: Channel]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||