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2b3g

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{{STRUCTURE_2b3g| PDB=2b3g | SCENE= }}
{{STRUCTURE_2b3g| PDB=2b3g | SCENE= }}
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'''p53N (fragment 33-60) bound to RPA70N'''
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===p53N (fragment 33-60) bound to RPA70N===
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==Overview==
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One of many protein-protein interactions modulated upon DNA damage is that of the single-stranded DNA-binding protein, replication protein A (RPA), with the p53 tumor suppressor. Here we report the crystal structure of RPA residues 1-120 (RPA70N) bound to the N-terminal transactivation domain of p53 (residues 37-57; p53N) and, by using NMR spectroscopy, characterize two mechanisms by which the RPA/p53 interaction can be modulated. RPA70N forms an oligonucleotide/oligosaccharide-binding fold, similar to that previously observed for the ssDNA-binding domains of RPA. In contrast, the N-terminal p53 transactivation domain is largely disordered in solution, but residues 37-57 fold into two amphipathic helices, H1 and H2, upon binding with RPA70N. The H2 helix of p53 structurally mimics the binding of ssDNA to the oligonucleotide/oligosaccharide-binding fold. NMR experiments confirmed that both ssDNA and an acidic peptide mimicking a phosphorylated form of RPA32N can independently compete the acidic p53N out of the binding site. Taken together, our data suggest a mechanism for DNA damage signaling that can explain a threshold response to DNA damage.
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{{ABSTRACT_PUBMED_16234232}}
==About this Structure==
==About this Structure==
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[[Category: Ob-fold]]
[[Category: Ob-fold]]
[[Category: Ssdna mimicry]]
[[Category: Ssdna mimicry]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:48:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:16:13 2008''

Revision as of 21:16, 27 July 2008

Image:2b3g.png

Template:STRUCTURE 2b3g

p53N (fragment 33-60) bound to RPA70N

Template:ABSTRACT PUBMED 16234232

About this Structure

2B3G is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A., Bochkareva E, Kaustov L, Ayed A, Yi GS, Lu Y, Pineda-Lucena A, Liao JC, Okorokov AL, Milner J, Arrowsmith CH, Bochkarev A, Proc Natl Acad Sci U S A. 2005 Oct 25;102(43):15412-7. Epub 2005 Oct 17. PMID:16234232

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