1xox

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(New page: 200px<br /> <applet load="1xox" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xox" /> '''SOLUTION STRUCTURE OF HUMAN SURVIVIN'''<br ...)
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<applet load="1xox" size="450" color="white" frame="true" align="right" spinBox="true"
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'''SOLUTION STRUCTURE OF HUMAN SURVIVIN'''<br />
'''SOLUTION STRUCTURE OF HUMAN SURVIVIN'''<br />
==Overview==
==Overview==
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NMR studies of the antiapoptotic protein survivin have been used to, determine the homodimer interface of the protein in solution and to, identify residues of the protein that interact with Smac/Diablo. In, solution, survivin(1-120) forms a bow-tie-shaped dimer whose interface is, composed of its N-terminal residues as well as residues connecting its BIR, domain to the C-terminal alpha helix. The solution structure resolves the, controversy regarding the two possible dimer interfaces for survivin, observed in X-ray crystal structures. The structural basis for the, interaction between survivin and Smac/Diablo was also investigated. When, Smac/Diablo or N-terminal Smac/Diablo peptide analogues are added to a, solution of survivin, specific residues near alpha4 and beta3 are, perturbed. NMR experiments indicate that the peptides bind across the, third beta-strand of survivin in a manner similar to the way Smac/Diablo, peptides bind to the BIR3 domain of X-linked IAP (XIAP).
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NMR studies of the antiapoptotic protein survivin have been used to determine the homodimer interface of the protein in solution and to identify residues of the protein that interact with Smac/Diablo. In solution, survivin(1-120) forms a bow-tie-shaped dimer whose interface is composed of its N-terminal residues as well as residues connecting its BIR domain to the C-terminal alpha helix. The solution structure resolves the controversy regarding the two possible dimer interfaces for survivin observed in X-ray crystal structures. The structural basis for the interaction between survivin and Smac/Diablo was also investigated. When Smac/Diablo or N-terminal Smac/Diablo peptide analogues are added to a solution of survivin, specific residues near alpha4 and beta3 are perturbed. NMR experiments indicate that the peptides bind across the third beta-strand of survivin in a manner similar to the way Smac/Diablo peptides bind to the BIR3 domain of X-linked IAP (XIAP).
==About this Structure==
==About this Structure==
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1XOX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XOX OCA].
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1XOX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOX OCA].
==Reference==
==Reference==
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[[Category: Liu, Z.]]
[[Category: Liu, Z.]]
[[Category: Nettesheim, D.]]
[[Category: Nettesheim, D.]]
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[[Category: Olejniczak, E.T.]]
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[[Category: Olejniczak, E T.]]
[[Category: Sun, C.]]
[[Category: Sun, C.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: bir domain; apoptosis]]
[[Category: bir domain; apoptosis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:08:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:04 2008''

Revision as of 13:57, 21 February 2008


1xox

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SOLUTION STRUCTURE OF HUMAN SURVIVIN

Overview

NMR studies of the antiapoptotic protein survivin have been used to determine the homodimer interface of the protein in solution and to identify residues of the protein that interact with Smac/Diablo. In solution, survivin(1-120) forms a bow-tie-shaped dimer whose interface is composed of its N-terminal residues as well as residues connecting its BIR domain to the C-terminal alpha helix. The solution structure resolves the controversy regarding the two possible dimer interfaces for survivin observed in X-ray crystal structures. The structural basis for the interaction between survivin and Smac/Diablo was also investigated. When Smac/Diablo or N-terminal Smac/Diablo peptide analogues are added to a solution of survivin, specific residues near alpha4 and beta3 are perturbed. NMR experiments indicate that the peptides bind across the third beta-strand of survivin in a manner similar to the way Smac/Diablo peptides bind to the BIR3 domain of X-linked IAP (XIAP).

About this Structure

1XOX is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of human survivin and its binding interface with Smac/Diablo., Sun C, Nettesheim D, Liu Z, Olejniczak ET, Biochemistry. 2005 Jan 11;44(1):11-7. PMID:15628841

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