1xpa

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==Overview==
==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.
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.
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==Disease==
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Known diseases associated with this structure: Xeroderma pigmentosum, group A OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611153 611153]]
==About this Structure==
==About this Structure==
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[[Category: zinc-finger]]
[[Category: zinc-finger]]
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Revision as of 18:02, 12 November 2007


1xpa

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SOLUTION STRUCTURE OF THE DNA-AND RPA-BINDING DOMAIN OF THE HUMAN REPAIR FACTOR XPA, NMR, 1 STRUCTURE

Contents

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.

Disease

Known diseases associated with this structure: Xeroderma pigmentosum, group A OMIM:[611153]

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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