1XPA

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

Summary for 1XPA

• Entry DOI: 10.2210/pdb1xpa/pdb
• NMR Information: BMRB: 4249
• Descriptor: XPA, ZINC ION (2 entities in total)
• Functional Keywords: dna repair, nucleotide excision repair, zinc-finger
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P23025
• Total number of polymer chains: 1
• Total formula weight: 14794.39

Authors

Ikegami, T.,Kuraoka, I.,Saijo, M.,Kodo, N.,Kyogoku, Y.,Morikawa, K.,Tanaka, K.,Shirakawa, M. (deposition date: 1998-07-06, release date: 1999-07-22, Last modification date: 2024-05-22)

Primary citation

Ikegami, T.,Kuraoka, I.,Saijo, M.,Kodo, N.,Kyogoku, Y.,Morikawa, K.,Tanaka, K.,Shirakawa, M.
Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA.
Nat.Struct.Biol., 5:701-706, 1998

PubMed Abstract: 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.

PubMed: 9699634
DOI: 10.1038/1400

Experimental method

SOLUTION NMR