Five atomic resolution structures of endothiapepsin inhibitor complexes: Implications for the aspartic proteinase mechanism

Journal of Molecular Biology

Volumn 318, Issue 5, 2002, Pages 1405-1415

  Coates, L ^a   Erskine, P T ^a   Crump, M P ^a   Wood, S P ^a   Cooper, J B ^a  

^a UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

Author keywords

Anisotropic refinement; Aspartic proteinase mechanism; Atomic resolution; Tetrahedral intermediate; Transition state analogues

Indexed keywords

ASPARTIC ACID; ASPARTIC PROTEINASE; CARBONYL DERIVATIVE; ENDOTHIAPEPSIN; ENZYME INHIBITOR; H 189; H 256; HYDROGEN; OXYGEN; PD 129541; PD 130328; PROTON; TERLAKIREN; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ANISOTROPY; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME DEGRADATION; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING;

CRYPHONECTRIA PARASITICA; ENDOTHIA; FUNGI; TEREBRANTIA;

EID: 0036311072     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00197-3     Document Type: Article

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