1g5j
From Proteopedia
(New page: 200px<br /> <applet load="1g5j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g5j" /> '''COMPLEX OF BCL-XL WITH PEPTIDE FROM BAD'''<...) |
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| - | [[Image:1g5j.gif|left|200px]]<br /> | + | [[Image:1g5j.gif|left|200px]]<br /><applet load="1g5j" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1g5j" size=" | + | |
caption="1g5j" /> | caption="1g5j" /> | ||
'''COMPLEX OF BCL-XL WITH PEPTIDE FROM BAD'''<br /> | '''COMPLEX OF BCL-XL WITH PEPTIDE FROM BAD'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the anti-apoptotic protein Bcl-xL | + | The three-dimensional structure of the anti-apoptotic protein Bcl-xL complexed to a 25-residue peptide from the death promoting region of Bad was determined using NMR spectroscopy. Although the overall structure is similar to Bcl-xL bound to a 16-residue peptide from the Bak protein (Sattler et al., 1997), the Bad peptide forms additional interactions with Bcl-xL. However, based upon site-directed mutagenesis experiments, these additional contacts do not account for the increased affinity of the Bad 25-mer for Bcl-xL compared to the Bad 16-mer. Rather, the increased helix propensity of the Bad 25-mer is primarily responsible for its greater affinity for Bcl-xL. Based on this observation, a pair of 16-residue peptides were designed and synthesized that were predicted to have a high helix propensity while maintaining the interactions important for complexation with Bcl-xL. Both peptides showed an increase in helix propensity compared to the wild-type and exhibited an enhanced affinity for Bcl-xL. |
==About this Structure== | ==About this Structure== | ||
| - | 1G5J is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1G5J is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1G5J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Fesik, S | + | [[Category: Fesik, S W.]] |
[[Category: Mack, J.]] | [[Category: Mack, J.]] | ||
| - | [[Category: Matayoshi, E | + | [[Category: Matayoshi, E D.]] |
| - | [[Category: Meadows, R | + | [[Category: Meadows, R P.]] |
| - | [[Category: Nettesheim, D | + | [[Category: Nettesheim, D G.]] |
| - | [[Category: Olejniczak, E | + | [[Category: Olejniczak, E T.]] |
| - | [[Category: Petros, A | + | [[Category: Petros, A M.]] |
[[Category: Swift, K.]] | [[Category: Swift, K.]] | ||
| - | [[Category: Thompson, C | + | [[Category: Thompson, C B.]] |
[[Category: Wang, Y.]] | [[Category: Wang, Y.]] | ||
[[Category: Zhang, H.]] | [[Category: Zhang, H.]] | ||
[[Category: complex]] | [[Category: complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:21 2008'' |
Revision as of 10:46, 21 February 2008
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COMPLEX OF BCL-XL WITH PEPTIDE FROM BAD
Overview
The three-dimensional structure of the anti-apoptotic protein Bcl-xL complexed to a 25-residue peptide from the death promoting region of Bad was determined using NMR spectroscopy. Although the overall structure is similar to Bcl-xL bound to a 16-residue peptide from the Bak protein (Sattler et al., 1997), the Bad peptide forms additional interactions with Bcl-xL. However, based upon site-directed mutagenesis experiments, these additional contacts do not account for the increased affinity of the Bad 25-mer for Bcl-xL compared to the Bad 16-mer. Rather, the increased helix propensity of the Bad 25-mer is primarily responsible for its greater affinity for Bcl-xL. Based on this observation, a pair of 16-residue peptides were designed and synthesized that were predicted to have a high helix propensity while maintaining the interactions important for complexation with Bcl-xL. Both peptides showed an increase in helix propensity compared to the wild-type and exhibited an enhanced affinity for Bcl-xL.
About this Structure
1G5J is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies., Petros AM, Nettesheim DG, Wang Y, Olejniczak ET, Meadows RP, Mack J, Swift K, Matayoshi ED, Zhang H, Thompson CB, Fesik SW, Protein Sci. 2000 Dec;9(12):2528-34. PMID:11206074
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