1mk3
From Proteopedia
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| - | [[Image:1mk3.gif|left|200px]] | + | [[Image:1mk3.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF HUMAN BCL-W PROTEIN''' | + | {{Structure |
| + | |PDB= 1mk3 |SIZE=350|CAPTION= <scene name='initialview01'>1mk3</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF HUMAN BCL-W PROTEIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MK3 is a [ | + | 1MK3 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=1MK3 OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix., Denisov AY, Madiraju MS, Chen G, Khadir A, Beauparlant P, Attardo G, Shore GC, Gehring K, J Biol Chem. 2003 Jun 6;278(23):21124-8. Epub 2003 Mar 21. PMID:[http:// | + | Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix., Denisov AY, Madiraju MS, Chen G, Khadir A, Beauparlant P, Attardo G, Shore GC, Gehring K, J Biol Chem. 2003 Jun 6;278(23):21124-8. Epub 2003 Mar 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12651847 12651847] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Madiraju, M S.]] | [[Category: Madiraju, M S.]] | ||
[[Category: Shore, G C.]] | [[Category: Shore, G C.]] | ||
| - | [[Category: | + | [[Category: apoptoti]] |
[[Category: bcl-w protein]] | [[Category: bcl-w protein]] | ||
| - | ''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 12:44:25 2008'' |
Revision as of 10:44, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF HUMAN BCL-W PROTEIN
Overview
The structure of human BCL-w, an anti-apoptotic member of the BCL-2 family, was determined by triple-resonance NMR spectroscopy and molecular modeling. Introduction of a single amino acid substitution (P117V) significantly improved the quality of the NMR spectra obtained. The cytosolic domain of BCL-w consists of 8 alpha-helices, which adopt a fold similar to that of BCL-xL, BCL-2, and BAX proteins. Pairwise root meant square deviation values were less than 3 A for backbone atoms of structurally equivalent regions. Interestingly, the C-terminal helix alpha8 of BCL-w folds into the BH3-binding hydrophobic cleft of the protein, in a fashion similar to the C-terminal transmembrane helix of BAX. A peptide corresponding to the BH3 region of the pro-apoptotic protein, BID, could displace helix alpha8 from the BCL-w cleft, resulting in helix unfolding. Deletion of helix alpha8 increased binding affinities of BCL-w for BAK and BID BH3-peptides, indicating that this helix competes for peptide binding to the hydrophobic cleft. These results suggest that although the cytosolic domain of BCL-w exhibits an overall structure similar to that of BCL-xL and BCL-2, the unique organization of its C-terminal helix may modulate BCL-w interactions with pro-apoptotic binding partners.
About this Structure
1MK3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix., Denisov AY, Madiraju MS, Chen G, Khadir A, Beauparlant P, Attardo G, Shore GC, Gehring K, J Biol Chem. 2003 Jun 6;278(23):21124-8. Epub 2003 Mar 21. PMID:12651847
Page seeded by OCA on Thu Mar 20 12:44:25 2008
