Journal article
Interactions of Human Nucleotide Excision Repair Protein XPA with DNA and RPA70 Delta c327: Chemical Shift Mapping and N-15 NMR Relaxation Studies
Biochemistry, Vol.38(46), pp.15116-15128
12/28/1999
DOI: 10.1021/bi991755p
PMID: 10563794
Abstract
Human XPA is an essential component in the multienzyme nucleotide excision repair (NER) pathway. The solution structure of the minimal DNA binding domain of XPA (XPA-MBD: M98-F219) was recently determined [Buchko et al. (1998) Nucleic Acids Res. 26, 2779-2788, Ikegami et al (1998) Nat. Struct. Biol. 5, 701-706] and shown to consist of a compact zinc-binding core and a loop-rich C-terminal subdomain connected by a linker sequence.
Details
- Title: Subtitle
- Interactions of Human Nucleotide Excision Repair Protein XPA with DNA and RPA70 Delta c327: Chemical Shift Mapping and N-15 NMR Relaxation Studies
- Creators
- Garry W BuchkoGary W DaughdrillRobert De LorimierSudha Rao B KNancy G IsernJody M LingbeckJohn-Stephen TaylorMarc S WoldMiriam GochinLeonard D SpicerDavid F LowryMichael A Kennedy
- Resource Type
- Journal article
- Publication Details
- Biochemistry, Vol.38(46), pp.15116-15128
- DOI
- 10.1021/bi991755p
- PMID
- 10563794
- NLM abbreviation
- Biochemistry
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Publisher
- United States
- Language
- English
- Date published
- 12/28/1999
- Academic Unit
- Radiation Oncology; Biochemistry and Molecular Biology
- Record Identifier
- 9984024419602771
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