2vge

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{{STRUCTURE_2vge| PDB=2vge | SCENE= }}
{{STRUCTURE_2vge| PDB=2vge | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE C-TERMINAL REGION OF HUMAN IASPP'''
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===CRYSTAL STRUCTURE OF THE C-TERMINAL REGION OF HUMAN IASPP===
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==Overview==
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ASPP1 and ASPP2 are activators of p53-dependent apoptosis, whereas iASPP is an inhibitor of p53. Binding assays showed differential binding for C-terminal domains of iASPP and ASPP2 to the core domains of p53 family members p53, p63, and p73. We also determined a high-resolution crystal structure for the C terminus of iASPP, comprised of four ankyrin repeats and an SH3 domain. The crystal lattice revealed an interaction between eight sequential residues in one iASPP molecule and the p53-binding site of a neighboring molecule. ITC confirmed that a peptide corresponding to the crystallographic interaction shows specific binding to iASPP. The contributions of ankyrin repeat residues, in addition to those of the SH3 domain, generate distinctive architecture at the p53-binding site suitable for inhibition by small molecules. These results suggest that the binding properties of iASPP render it a target for antitumor therapeutics and provide a peptide-based template for compound design.
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(as it appears on PubMed at http://www.pubmed.gov), where 18275817 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18275817}}
==About this Structure==
==About this Structure==
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:45:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:05:39 2008''

Revision as of 05:05, 28 July 2008

Image:2vge.png

Template:STRUCTURE 2vge

CRYSTAL STRUCTURE OF THE C-TERMINAL REGION OF HUMAN IASPP

Template:ABSTRACT PUBMED 18275817

About this Structure

2VGE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Biochemical and Structural Studies of ASPP Proteins Reveal Differential Binding to p53, p63, and p73., Robinson RA, Lu X, Jones EY, Siebold C, Structure. 2008 Feb;16(2):259-68. PMID:18275817

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