2f37

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==Overview==
==Overview==
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TRPV channels are important polymodal integrators of noxious stimuli, mediating thermosensation and nociception. An ankyrin repeat domain (ARD), which is a common protein-protein recognition domain, is conserved in the, N-terminal intracellular domain of all TRPV channels and predicted to, contain three to four ankyrin repeats. Here we report the first structure, from the TRPV channel subfamily, a 1.7 A resolution crystal structure of, the human TRPV2 ARD. Our crystal structure reveals a six ankyrin repeat, stack with multiple insertions in each repeat generating several unique, features compared with a canonical ARD. The surface typically used for, ligand recognition, the ankyrin groove, contains extended loops with an, exposed hydrophobic patch and a prominent kink resulting from a large, rotational shift of the last two repeats. The TRPV2 ARD provides the first, structural insight into a domain that coordinates nociceptive sensory, transduction and is likely to be a prototype for other TRPV channel ARDs.
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TRPV channels are important polymodal integrators of noxious stimuli mediating thermosensation and nociception. An ankyrin repeat domain (ARD), which is a common protein-protein recognition domain, is conserved in the N-terminal intracellular domain of all TRPV channels and predicted to contain three to four ankyrin repeats. Here we report the first structure from the TRPV channel subfamily, a 1.7 A resolution crystal structure of the human TRPV2 ARD. Our crystal structure reveals a six ankyrin repeat stack with multiple insertions in each repeat generating several unique features compared with a canonical ARD. The surface typically used for ligand recognition, the ankyrin groove, contains extended loops with an exposed hydrophobic patch and a prominent kink resulting from a large rotational shift of the last two repeats. The TRPV2 ARD provides the first structural insight into a domain that coordinates nociceptive sensory transduction and is likely to be a prototype for other TRPV channel ARDs.
==About this Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: McCleverty, C.J.]]
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[[Category: McCleverty, C J.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: ankyrin repeat]]
[[Category: ankyrin repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:24:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:17:16 2008''

Revision as of 15:17, 21 February 2008


2f37, resolution 1.70Å

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Crystal structure of the ankyrin repeat domain of human TRPV2

Overview

TRPV channels are important polymodal integrators of noxious stimuli mediating thermosensation and nociception. An ankyrin repeat domain (ARD), which is a common protein-protein recognition domain, is conserved in the N-terminal intracellular domain of all TRPV channels and predicted to contain three to four ankyrin repeats. Here we report the first structure from the TRPV channel subfamily, a 1.7 A resolution crystal structure of the human TRPV2 ARD. Our crystal structure reveals a six ankyrin repeat stack with multiple insertions in each repeat generating several unique features compared with a canonical ARD. The surface typically used for ligand recognition, the ankyrin groove, contains extended loops with an exposed hydrophobic patch and a prominent kink resulting from a large rotational shift of the last two repeats. The TRPV2 ARD provides the first structural insight into a domain that coordinates nociceptive sensory transduction and is likely to be a prototype for other TRPV channel ARDs.

About this Structure

2F37 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human TRPV2 channel ankyrin repeat domain., McCleverty CJ, Koesema E, Patapoutian A, Lesley SA, Kreusch A, Protein Sci. 2006 Sep;15(9):2201-6. Epub 2006 Aug 1. PMID:16882997

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