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1xpa
From Proteopedia
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Revision as of 15:27, 5 November 2007
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SOLUTION STRUCTURE OF THE DNA-AND RPA-BINDING DOMAIN OF THE HUMAN REPAIR FACTOR XPA, NMR, 1 STRUCTURE
Overview
The solution structure of the central domain of the human nucleotide, excision repair protein XPA, which binds to damaged DNA and replication, protein A (RPA), was determined by nuclear magnetic resonance (NMR), spectroscopy. The central domain consists of a zinc-containing subdomain, and a C-terminal subdomain. The zinc-containing subdomain has a compact, globular structure and is distinct from the zinc-fingers found in, transcription factors. The C-terminal subdomain folds into a novel, alpha/beta structure with a positively charged superficial cleft. From the, NMR spectra of the complexes, DNA and RPA binding surfaces are suggested.
About this Structure
1XPA is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Structure known Active Site: NUL. Full crystallographic information is available from OCA.
Reference
Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA., Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M, Nat Struct Biol. 1998 Aug;5(8):701-6. PMID:9699634
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