Crystal structure of the thrombin mutant D221A/D222K: The Asp222:Arg187 ion-pair stabilizes the fast form

Biophysical Chemistry

Volumn 112, Issue 2-3 SPEC. ISS., 2004, Pages 253-256

  Pineda, Agustin O ^a   Zhang, Erli ^b   Guinto, Enriqueta R ^a   Savvides, Savvas N ^a   Tulinsky, Alexander ^b   Di Cera, Enrico ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b MICHIGAN STATE UNIVERSITY   (United States)

Author keywords

Allostery; Na + binding; Serine protease structure; Thrombin

Indexed keywords

ARGININE; ASPARTIC ACID; HIRUDIN; LYSINE; MUTANT PROTEIN; OXYGEN; SODIUM; SOLVENT; THROMBIN;

ARTICLE; ATOM; BINDING AFFINITY; BINDING SITE; CONFORMATION; CRYSTAL STRUCTURE; MOLECULAR INTERACTION; MOLECULE; PRIORITY JOURNAL; WILD TYPE; X RAY ANALYSIS;

BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; FACTOR XA; MODELS, MOLECULAR; MOLECULAR MIMICRY; MUTATION, MISSENSE; PROTEIN CONFORMATION; SODIUM; THROMBIN;

EID: 9644257386     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2004.07.027     Document Type: Article

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