1r2h

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{{STRUCTURE_1r2h| PDB=1r2h | SCENE= }}
{{STRUCTURE_1r2h| PDB=1r2h | SCENE= }}
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'''Human Bcl-XL containing an Ala to Leu mutation at position 142'''
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===Human Bcl-XL containing an Ala to Leu mutation at position 142===
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==Overview==
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Cells expressing high levels of the BCL-X(L) anti-apoptotic protein are preferentially killed by the mitochondrial inhibitor antimycin A (AA). Computational modeling predicts a binding site for AA in the extended hydrophobic groove on BCL-X(L), previously identified as an interface for dimerization to BAX and related proapoptotic proteins. Here, we identify BCL-X(L) hydrophobic groove mutants with normal cellular anti-apoptotic function but suppressed sensitivity to AA. The LD(50) of AA for cells expressing BCL-X(L) mutants directly correlates with the measured in vitro dissociation constants for AA binding. These results indicate that BCL-X(L) is a principal target mediating AA cytotoxicity.
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(as it appears on PubMed at http://www.pubmed.gov), where 14534311 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14534311}}
==About this Structure==
==About this Structure==
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[[Category: Monomeric]]
[[Category: Monomeric]]
[[Category: Mutation]]
[[Category: Mutation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:59:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:37:42 2008''

Revision as of 04:37, 29 July 2008

Template:STRUCTURE 1r2h

Human Bcl-XL containing an Ala to Leu mutation at position 142

Template:ABSTRACT PUBMED 14534311

About this Structure

1R2H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Bcl-XL mutations suppress cellular sensitivity to antimycin A., Manion MK, O'Neill JW, Giedt CD, Kim KM, Zhang KY, Hockenbery DM, J Biol Chem. 2004 Jan 16;279(3):2159-65. Epub 2003 Oct 8. PMID:14534311

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