3u1c

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{{STRUCTURE_3u1c| PDB=3u1c | SCENE= }}
{{STRUCTURE_3u1c| PDB=3u1c | SCENE= }}
===Anti-parallel dimer of N-terminal 98-aa fragment of smooth muscle tropomyosin alpha===
===Anti-parallel dimer of N-terminal 98-aa fragment of smooth muscle tropomyosin alpha===
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{{ABSTRACT_PUBMED_022119916}}
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{{ABSTRACT_PUBMED_22119916}}
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==Function==
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[[http://www.uniprot.org/uniprot/TPM1_CHICK TPM1_CHICK]] Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
==About this Structure==
==About this Structure==
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==See Also==
==See Also==
*[[Tropomyosin|Tropomyosin]]
*[[Tropomyosin|Tropomyosin]]
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==Reference==
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<ref group="xtra">PMID:022119916</ref><references group="xtra"/><references/>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Dominguez, R.]]
[[Category: Dominguez, R.]]

Revision as of 08:47, 4 September 2013

Template:STRUCTURE 3u1c

Contents

Anti-parallel dimer of N-terminal 98-aa fragment of smooth muscle tropomyosin alpha

Template:ABSTRACT PUBMED 22119916

Function

[TPM1_CHICK] Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.

About this Structure

3u1c is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA.

See Also

Reference

  • Rao JN, Rivera-Santiago R, Li XE, Lehman W, Dominguez R. Structural analysis of smooth muscle tropomyosin alpha and beta isoforms. J Biol Chem. 2012 Jan 27;287(5):3165-74. Epub 2011 Nov 27. PMID:22119916 doi:10.1074/jbc.M111.307330

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