2g5b

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(New page: 200px<br /> <applet load="2g5b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g5b, resolution 2.300&Aring;" /> '''Crystal Structure ...)
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Revision as of 07:42, 18 November 2007

Image:2g5b.gif

2g5b, resolution 2.300Å

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Crystal Structure of the anti-Bax monoclonal antibody 6A7 and a Bax peptide.

Overview

The Bcl-2 family member Bax plays a critical role in apoptosis. In healthy, resting cells, Bax resides in the cytoplasm and loosely attached to the, mitochondrial membrane. Apoptotic stimuli induce Bax activation, which is, characterized by translocation and multimerization on the mitochondrial, membrane surface resulting in exposure of an amino terminal epitope, recognized by the monoclonal antibody 6A7. To understand the structural, changes that occur during Bax activation, we determined the crystal, structure of a Bax peptide bound to the 6A7 Fab fragment to a resolution, of 2.3 A. The structure reveals the conformation of the 6A7 peptide, epitope on Bax in the activated form and elucidates the extensive, structural changes that Bax must undergo during the conversion from its, native to its activated conformation.

About this Structure

2G5B is a Protein complex structure of sequences from Mus musculus with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

Elucidation of some Bax conformational changes through crystallization of an antibody-peptide complex., Peyerl FW, Dai S, Murphy GA, Crawford F, White J, Marrack P, Kappler JW, Cell Death Differ. 2007 Mar;14(3):447-52. Epub 2006 Sep 1. PMID:16946732

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