4m3l

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'''Unreleased structure'''
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{{STRUCTURE_4m3l| PDB=4m3l | SCENE= }}
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===Crystal Structure of the coiled coil domain of MuRF1===
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The entry 4m3l is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/TRI63_HUMAN TRI63_HUMAN]] E3 ubiquitin ligase. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.<ref>PMID:11927605</ref>
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Authors: Mayans, O., Franke, B.
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==About this Structure==
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[[4m3l]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M3L OCA].
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Description: Crystal Structure of the coiled coil domain of MuRF1
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Franke, B.]]
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[[Category: Mayans, O.]]
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[[Category: E3 ubiquitin ligase]]
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[[Category: Ligase]]
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[[Category: Sarcoskeleton]]
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[[Category: Titin]]

Revision as of 09:34, 26 March 2014

Template:STRUCTURE 4m3l

Contents

Crystal Structure of the coiled coil domain of MuRF1

Function

[TRI63_HUMAN] E3 ubiquitin ligase. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.[1]

About this Structure

4m3l is a 4 chain structure. Full crystallographic information is available from OCA.

Reference

  1. ↑ McElhinny AS, Kakinuma K, Sorimachi H, Labeit S, Gregorio CC. Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. J Cell Biol. 2002 Apr 1;157(1):125-36. Epub 2002 Apr 1. PMID:11927605 doi:http://dx.doi.org/10.1083/jcb.200108089

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OCA

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