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1kn0

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{{STRUCTURE_1kn0| PDB=1kn0 | SCENE= }}
{{STRUCTURE_1kn0| PDB=1kn0 | SCENE= }}
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'''Crystal Structure of the human Rad52 protein'''
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===Crystal Structure of the human Rad52 protein===
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==Overview==
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The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing, and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a beta-beta-beta-alpha fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the beta-beta-beta-alpha fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.
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(as it appears on PubMed at http://www.pubmed.gov), where 12191481 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12191481}}
==About this Structure==
==About this Structure==
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[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:34:39 2008''

Revision as of 07:34, 2 July 2008

Image:1kn0.png

Template:STRUCTURE 1kn0

Crystal Structure of the human Rad52 protein

Template:ABSTRACT PUBMED 12191481

About this Structure

1KN0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form., Kagawa W, Kurumizaka H, Ishitani R, Fukai S, Nureki O, Shibata T, Yokoyama S, Mol Cell. 2002 Aug;10(2):359-71. PMID:12191481

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