1rc9: Difference between revisions

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[[Image:1rc9.png|left|200px]]
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===Crystal Structure of Stecrisp, a Member of CRISP Family from Trimeresurus Stejnegeri Refined at 1.6 Angstroms Resolution: Structual relationship of the two domains===
===Crystal Structure of Stecrisp, a Member of CRISP Family from Trimeresurus Stejnegeri Refined at 1.6 Angstroms Resolution: Structual relationship of the two domains===
{{ABSTRACT_PUBMED_15596436}}


 
==Function==
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[[http://www.uniprot.org/uniprot/CRVP_TRIST CRVP_TRIST]] Blocks contraction of smooth muscle elicited by high potassium-induced depolarization, but does not block caffein-stimulated contraction. May target voltage-gated calcium channels on smooth muscle (By similarity).
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{{ABSTRACT_PUBMED_15596436}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:015596436</ref><references group="xtra"/>
<ref group="xtra">PMID:015596436</ref><references group="xtra"/><references/>
[[Category: Viridovipera stejnegeri]]
[[Category: Viridovipera stejnegeri]]
[[Category: Guo, M.]]
[[Category: Guo, M.]]

Revision as of 10:52, 16 April 2014

Template:STRUCTURE 1rc9

Crystal Structure of Stecrisp, a Member of CRISP Family from Trimeresurus Stejnegeri Refined at 1.6 Angstroms Resolution: Structual relationship of the two domains

Template:ABSTRACT PUBMED 15596436

Function

[CRVP_TRIST] Blocks contraction of smooth muscle elicited by high potassium-induced depolarization, but does not block caffein-stimulated contraction. May target voltage-gated calcium channels on smooth muscle (By similarity).

About this Structure

1rc9 is a 1 chain structure with sequence from Viridovipera stejnegeri. Full crystallographic information is available from OCA.

Reference

  1. Guo M, Teng M, Niu L, Liu Q, Huang Q, Hao Q. Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold. J Biol Chem. 2005 Apr 1;280(13):12405-12. Epub 2004 Dec 13. PMID:15596436 doi:10.1074/jbc.M413566200

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