Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides

Protein Science

Volumn 12, Issue 8, 2003, Pages 1741-1749

  Erskine, Peter T ^a   Coates, Leighton ^a   Mall, Sanjay ^a   Gill, Raj S ^a   Wood, Steve P ^a   Myles, Dean A A ^b   Cooper, Jon B ^a  

^a UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

^b INSTITUT LAUE LANGEVIN   (France)

Author keywords

Aspartic proteinase; Atomic resolution; Inhibition; Low barrier hydrogen bonds; Protonation state; Slow binding; Succinimide; Transpeptidation

Indexed keywords

ASPARTIC ACID; ASPARTIC PROTEINASE; BETA SECRETASE; DIPEPTIDE; ENDOTHIAPEPSIN; H 261; LYSOSOME ENZYME; OLIGOPEPTIDE; SERINE; THREONINE;

ANALYTIC METHOD; ARTICLE; AUTOLYSIS; BINDING AFFINITY; BINDING SITE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; COMPLEX FORMATION; COVALENT BOND; CRYSTALLIZATION; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; HYDROGEN BOND; METABOLISM; NONHUMAN; PEPTIDE ANALYSIS; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN BINDING; PROTON TRANSPORT; X RAY CRYSTALLOGRAPHY;

ASPARTIC ENDOPEPTIDASES; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DIPEPTIDES; ELECTROSTATICS; HYDROGEN BONDING; MODELS, MOLECULAR; OLIGOPEPTIDES; PROTEIN BINDING;

EID: 0041341883     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0305203     Document Type: Article

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