2m5b

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m (Protected "2m5b" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_2m5b| PDB=2m5b | SCENE= }}
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===The NMR structure of the BID-BAK complex===
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The entry 2m5b is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/BAK_HUMAN BAK_HUMAN]] In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis.<ref>PMID:8521816</ref> <ref>PMID:17157251</ref>
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Authors: Grace, C.R., Kriwacki, R.W., Green, D.R.
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==About this Structure==
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[[2m5b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M5B OCA].
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Description: The NMR structure of the BID-BAK complex
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Grace, C R.]]
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[[Category: Green, D R.]]
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[[Category: Kriwacki, R W.]]
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[[Category: Moldoveanu, T.]]
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[[Category: Apoptosis]]
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[[Category: Bcl-2 family effector bak]]
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[[Category: Bh3-only protein bid]]
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[[Category: Effector direct activation]]
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[[Category: Mitochondrial outer membrane premeabilization]]
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[[Category: Nmr solution structure of bid-bak complex]]

Revision as of 20:29, 17 April 2013

Template:STRUCTURE 2m5b

Contents

The NMR structure of the BID-BAK complex

Function

[BAK_HUMAN] In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis.[1] [2]

About this Structure

2m5b is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

  1. ↑ Chittenden T, Flemington C, Houghton AB, Ebb RG, Gallo GJ, Elangovan B, Chinnadurai G, Lutz RJ. A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions. EMBO J. 1995 Nov 15;14(22):5589-96. PMID:8521816
  2. ↑ Moldoveanu T, Liu Q, Tocilj A, Watson M, Shore G, Gehring K. The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site. Mol Cell. 2006 Dec 8;24(5):677-88. PMID:17157251 doi:10.1016/j.molcel.2006.10.014

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