The DNA-binding domain of human papillomavirus type 18 E1: Crystal structure, dimerization, and DNA binding

Journal of Biological Chemistry

Volumn 279, Issue 5, 2004, Pages 3733-3742

  Auster, Anitra S ^a,b   Joshua Tor, Leemor ^a  

^a Howard Hughes Medical Institute Cold Spring Harbor Laboratory Cold Spring Harbor   (United States)

^b STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; DIMERIZATION; DNA; HYDROPHOBICITY; MONOMERS; TUMORS;

HYDROPHOBIC RESIDUES;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATASE; DNA; DNA BINDING PROTEIN; E1 PROTEIN, BOVINE PAPILLOMAVIRUS; GLUTATHIONE TRANSFERASE; HELICASE; HYBRID PROTEIN; ONCOGENE PROTEIN E1, HUMAN PAPILLOMAVIRUS TYPE 18; ONCOPROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ALPHA HELIX; ANIMAL CELL; ARTICLE; BASE PAIRING; BINDING COMPETITION; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTAL STRUCTURE; DIMERIZATION; DNA BINDING; DNA REPLICATION; ENZYME ACTIVITY; HIGH RISK PATIENT; HUMAN; HYDROGEN BOND; HYDROPHOBICITY; METABOLISM; MOLECULAR GENETICS; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; SERODIAGNOSIS; SITE DIRECTED MUTAGENESIS; UTERINE CERVIX CARCINOMA; WART VIRUS; WESTERN BLOTTING; X RAY CRYSTALLOGRAPHY;

BASE SEQUENCE; BINDING, COMPETITIVE; BLOTTING, WESTERN; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DNA; DNA-BINDING PROTEINS; GLUTATHIONE TRANSFERASE; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; ONCOGENE PROTEINS, VIRAL; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; VIRAL PROTEINS;

ANIMALIA; BOVINAE; BOVINE PAPILLOMAVIRUS; BOVINE PAPILLOMAVIRUS TYPE 1; BOVINE PARVOVIRUS; HUMAN PAPILLOMAVIRUS; HUMAN PAPILLOMAVIRUS TYPE 18; HUMAN PAPILLOMAVIRUS TYPES;

EID: 0942265512     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M311681200     Document Type: Article

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