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3j4k

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'''Unreleased structure'''
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{{STRUCTURE_3j4k| PDB=3j4k | SCENE= }}
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===Cryo-EM structures of the actin:tropomyosin filament reveal the mechanism for the transition from C- to M-state===
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{{ABSTRACT_PUBMED_24021812}}
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The entry 3j4k is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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Authors: Sousa, D.R., Stagg, S.M., Stroupe, M.E.
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==About this Structure==
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[[3j4k]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J4K OCA].
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Description: Cryo-EM structures of the actin:tropomyosin filament reveal the mechanism for the transition from C-to M-state
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==Reference==
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<ref group="xtra">PMID:024021812</ref><references group="xtra"/><references/>
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[[Category: Gallus gallus]]
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[[Category: Oryctolagus cuniculus]]
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[[Category: Sousa, D R.]]
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[[Category: Stagg, S M.]]
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[[Category: Stroupe, M E.]]
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[[Category: Actin]]
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[[Category: Coiled-coil c-state]]
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[[Category: Structural protein]]
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[[Category: Tropomyosin]]

Revision as of 08:08, 29 September 2013

Template:STRUCTURE 3j4k

Contents

Cryo-EM structures of the actin:tropomyosin filament reveal the mechanism for the transition from C- to M-state

Template:ABSTRACT PUBMED 24021812

Function

[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

About this Structure

3j4k is a 7 chain structure with sequence from Gallus gallus and Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

  • Sousa DR, Stagg SM, Stroupe ME. Cryo-EM Structures of the Actin:Tropomyosin Filament Reveal the Mechanism for the Transition from C- to M-State. J Mol Biol. 2013 Sep 8. pii: S0022-2836(13)00540-8. doi:, 10.1016/j.jmb.2013.08.020. PMID:24021812 doi:10.1016/j.jmb.2013.08.020

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OCA

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