1o0l: Difference between revisions
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[[Image:1o0l.gif|left|200px]] | [[Image:1o0l.gif|left|200px]] | ||
'''THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN MODULATING BIOLOGICAL ACTIVITY''' | {{Structure | ||
|PDB= 1o0l |SIZE=350|CAPTION= <scene name='initialview01'>1o0l</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= BCL2L2 OR BCLW OR KIAA0271 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN MODULATING BIOLOGICAL ACTIVITY''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1O0L is a [ | 1O0L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O0L OCA]. | ||
==Reference== | ==Reference== | ||
The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity., Hinds MG, Lackmann M, Skea GL, Harrison PJ, Huang DC, Day CL, EMBO J. 2003 Apr 1;22(7):1497-507. PMID:[http:// | The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity., Hinds MG, Lackmann M, Skea GL, Harrison PJ, Huang DC, Day CL, EMBO J. 2003 Apr 1;22(7):1497-507. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12660157 12660157] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helical bundle]] | [[Category: helical bundle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:04:10 2008'' | ||
Revision as of 11:04, 20 March 2008
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| Gene: | BCL2L2 OR BCLW OR KIAA0271 (Homo sapiens) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN MODULATING BIOLOGICAL ACTIVITY
Overview
Pro-survival Bcl-2-related proteins, critical regulators of apoptosis, contain a hydrophobic groove targeted for binding by the BH3 domain of the pro-apoptotic BH3-only proteins. The solution structure of the pro-survival protein Bcl-w, presented here, reveals that the binding groove is not freely accessible as predicted by previous structures of pro-survival Bcl-2-like molecules. Unexpectedly, the groove appears to be occluded by the C-terminal residues. Binding and kinetic data suggest that the C-terminal residues of Bcl-w and Bcl-x(L) modulate pro-survival activity by regulating ligand access to the groove. Binding of the BH3-only proteins, critical for cell death initiation, is likely to displace the hydrophobic C-terminal region of Bcl-w and Bcl-x(L). Moreover, Bcl-w does not act only by sequestering the BH3-only proteins. There fore, pro-survival Bcl-2-like molecules probably control the activation of downstream effectors by a mechanism that remains to be elucidated.
About this Structure
1O0L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity., Hinds MG, Lackmann M, Skea GL, Harrison PJ, Huang DC, Day CL, EMBO J. 2003 Apr 1;22(7):1497-507. PMID:12660157
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