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4m9r

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'''Unreleased structure'''
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{{STRUCTURE_4m9r| PDB=4m9r | SCENE= }}
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===Crystal structure of CED-3===
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{{ABSTRACT_PUBMED_24065769}}
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The entry 4m9r is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/CED3_CAEEL CED3_CAEEL]] Acts as a cysteine protease in controlling programmed cell death by proteolytically activating or inactivating a substrate protein or proteins, a potential substrate may be ced-4. Alternatively it might directly cause cell death by proteolytically cleaving proteins that are crucial for cell viability.
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Authors: Xu, Y., Jeffrey, P., Shi, Y.G.
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==About this Structure==
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[[4m9r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M9R OCA].
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Description: Crystal structure of CED-3
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==Reference==
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<ref group="xtra">PMID:024065769</ref><references group="xtra"/><references/>
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[[Category: Caenorhabditis elegans]]
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[[Category: Jeffrey, P D.]]
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[[Category: Shi, Y G.]]
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[[Category: Xu, Y.]]
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[[Category: Caspase]]
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[[Category: Ced-4]]
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[[Category: Hydrolase]]
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[[Category: Protease]]

Revision as of 06:27, 10 October 2013

Template:STRUCTURE 4m9r

Contents

Crystal structure of CED-3

Template:ABSTRACT PUBMED 24065769

Function

[CED3_CAEEL] Acts as a cysteine protease in controlling programmed cell death by proteolytically activating or inactivating a substrate protein or proteins, a potential substrate may be ced-4. Alternatively it might directly cause cell death by proteolytically cleaving proteins that are crucial for cell viability.

About this Structure

4m9r is a 2 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

  • Huang W, Jiang T, Choi W, Qi S, Pang Y, Hu Q, Xu Y, Gong X, Jeffrey PD, Wang J, Shi Y. Mechanistic insights into CED-4-mediated activation of CED-3. Genes Dev. 2013 Sep 15;27(18):2039-48. doi: 10.1101/gad.224428.113. PMID:24065769 doi:http://dx.doi.org/10.1101/gad.224428.113

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