1xpa

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|PDB= 1xpa |SIZE=350|CAPTION= <scene name='initialview01'>1xpa</scene>
|PDB= 1xpa |SIZE=350|CAPTION= <scene name='initialview01'>1xpa</scene>
|SITE= <scene name='pdbsite=NUL:Zn+Binding+Site'>NUL</scene>
|SITE= <scene name='pdbsite=NUL:Zn+Binding+Site'>NUL</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xpa OCA], [http://www.ebi.ac.uk/pdbsum/1xpa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xpa RCSB]</span>
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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: Shirakawa, M.]]
[[Category: Shirakawa, M.]]
[[Category: Tanaka, K.]]
[[Category: Tanaka, K.]]
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[[Category: ZN]]
 
[[Category: dna repair]]
[[Category: dna repair]]
[[Category: nucleotide excision repair]]
[[Category: nucleotide excision repair]]
[[Category: zinc-finger]]
[[Category: zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:52:44 2008''

Revision as of 21:52, 30 March 2008


PDB ID 1xpa

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Sites:
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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