2eta
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(New page: 200px<br /><applet load="2eta" size="450" color="white" frame="true" align="right" spinBox="true" caption="2eta, resolution 2.20Å" /> '''Crystal structure of...)
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Revision as of 08:00, 21 November 2007
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Crystal structure of the ankyrin repeat domain of the TRPV2
Overview
The TRPV ion channels mediate responses to many sensory stimuli including, heat, low pH, neuropeptides, and chemical ligands. All TRPV subfamily, members contain an intracellular N-terminal ankyrin repeat domain (ARD), a, prevalent protein interaction motif. The 1.6-A crystal structure of the, TRPV2-ARD, with six ankyrin repeats, reveals several atypical structural, features. Repeats one through three display unusually long and flexible, fingers with a large number of exposed aromatic residues, whereas repeats, five and six have unusually long outer helices. Furthermore, a large, counterclockwise twist observed in the stacking of repeats four and five, breaks the regularity of the domain, altering the shape of surfaces, available for interactions with proteins or other cellular ligands. Both, solution studies and crystal packing interactions indicate that the, TRPV2-ARD does not form homo-oligomers, suggesting that the ARD of TRPV, ion channels may be used for interactions with regulatory factors rather, than in promoting tetrameric assembly of the ion channels.
About this Structure
2ETA is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel., Jin X, Touhey J, Gaudet R, J Biol Chem. 2006 Sep 1;281(35):25006-10. Epub 2006 Jun 29. PMID:16809337
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