2pnn

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{{STRUCTURE_2pnn| PDB=2pnn | SCENE= }}
{{STRUCTURE_2pnn| PDB=2pnn | SCENE= }}
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'''Crystal Structure of the Ankyrin Repeat Domain of Trpv1'''
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===Crystal Structure of the Ankyrin Repeat Domain of Trpv1===
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==Overview==
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TRPV1 plays a key role in nociception, as it is activated by heat, low pH, and ligands such as capsaicin, leading to a burning pain sensation. We describe the structure of the cytosolic ankyrin repeat domain (ARD) of TRPV1 and identify a multiligand-binding site important in regulating channel sensitivity within the TRPV1-ARD. The structure reveals a binding site that accommodates triphosphate nucleotides such as ATP, and biochemical studies demonstrate that calmodulin binds the same site. Electrophysiology experiments show that either ATP or PIP2 prevent desensitization to repeated applications of capsaicin, i.e., tachyphylaxis, while calmodulin plays an opposing role and is necessary for tachyphylaxis. Mutations in the TRPV1-ARD binding site eliminate tachyphylaxis. We present a model for the calcium-dependent regulation of TRPV1 via competitive interactions of ATP and calmodulin at the TRPV1-ARD-binding site and discuss its relationship to the C-terminal region previously implicated in interactions with PIP2 and calmodulin.
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(as it appears on PubMed at http://www.pubmed.gov), where 17582331 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17582331}}
==About this Structure==
==About this Structure==
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[[Category: Ankyrin repeat domain]]
[[Category: Ankyrin repeat domain]]
[[Category: Trpv1]]
[[Category: Trpv1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:29:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:11:32 2008''

Revision as of 17:11, 28 July 2008

Template:STRUCTURE 2pnn

Crystal Structure of the Ankyrin Repeat Domain of Trpv1

Template:ABSTRACT PUBMED 17582331

About this Structure

2PNN is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity., Lishko PV, Procko E, Jin X, Phelps CB, Gaudet R, Neuron. 2007 Jun 21;54(6):905-18. PMID:17582331

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