Impact of low-frequency hotspot mutation R282Q on the structure of p53 DNA-binding domain as revealed by crystallography at 1.54 Å resolution

Acta Crystallographica Section D: Biological Crystallography

Volumn 64, Issue 5, 2008, Pages 471-477

  Tu, Chao ^a   Tan, Yu Hong ^b   Shaw, Gary ^a   Zhou, Zheng ^c   Bai, Yawen ^c   Luo, Ray ^b   Ji, Xinhua ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c NATIONAL CANCER INSTITUTE   (United States)

Author keywords

DNA binding domains; Hotspots; Low frequency mutations; p53; R282Q

Indexed keywords

PROTEIN P53;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; METHODOLOGY; MUTATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; CRYSTALLOGRAPHY, X-RAY; HUMANS; MODELS, MOLECULAR; MUTATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; TUMOR SUPPRESSOR PROTEIN P53;

EID: 43249084473     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444908003338     Document Type: Article

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