1f16
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(New page: 200px<br /> <applet load="1f16" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f16" /> '''SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTE...)
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Revision as of 14:41, 12 November 2007
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SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX
Contents |
Overview
Apoptosis is stimulated by the insertion of Bax from the cytosol into, mitochondrial membranes. The solution structure of Bax, including the, putative transmembrane domain at the C terminus, was determined in order, to understand the regulation of its subcellular location. Bax consists of, 9 alpha helices where the assembly of helices alpha1 through alpha 8, resembles that of the apoptosis inhibitor, Bcl-x(L). The C-terminal alpha, 9 helix occupies the hydrophobic pocket proposed previously to mediate, heterodimer formation and bioactivity of opposing members of the Bcl-2, family. The Bax structure shows that the orientation of helix alpha 9, provides simultaneous control over its mitochondrial targeting and dimer, formation.
Disease
Known diseases associated with this structure: Colorectal cancer OMIM:[600040], T-cell acute lymphoblastic leukemia OMIM:[600040]
About this Structure
1F16 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of Bax: coregulation of dimer formation and intracellular localization., Suzuki M, Youle RJ, Tjandra N, Cell. 2000 Nov 10;103(4):645-54. PMID:11106734
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