Exploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligands

Proteins: Structure, Function and Genetics

Volumn 32, Issue 3, 1998, Pages 350-361

  Champness, John N ^a   Bennett, Matthew S ^a   Wien, Frank ^a   Visse, Rob ^a,e   Summers, William C ^b   Herdewijn, Piet ^c   De Clercq, Erik ^c   Ostrowski, Tomasz ^c   Jarvest, Richard L ^d   Sanderson, Mark R ^a  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c REGA INSTITUTE FOR MEDICAL RESEARCH   (Belgium)

^d GLAXOSMITHKLINE   (United Kingdom)

^e LEIDEN UNIVERSITY   (Netherlands)

Author keywords

Antivirals; Drug binding; Drug target; Enzyme structure; Intermolecular interactions; Zovirax

Indexed keywords

ACICLOVIR; DNA POLYMERASE; PENCICLOVIR; THYMIDINE KINASE;

ARTICLE; BINDING AFFINITY; DRUG BINDING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; GENE MUTATION; GENE THERAPY; HERPES SIMPLEX VIRUS; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; X RAY CRYSTALLOGRAPHY;

ACYCLOVIR; ANTIVIRAL AGENTS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HERPESVIRUS 1, HUMAN; LIGANDS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; THYMIDINE KINASE;

EID: 0032529367     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980815)32:3<350::AID-PROT10>3.0.CO;2-8     Document Type: Article

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