On the active site protonation state in aspartic proteases: Implications for drug design

Current Pharmaceutical Design

Volumn 19, Issue 23, 2013, Pages 4257-4275

  Sussman, Fredy ^a   Carmen Villaverde, M ^a   Domínguez, José L ^a   Helena Danielson, U ^b  

^a UNIVERSITY OF SANTIAGO DE COMPOSTELA   (Spain)

^b UPPSALA UNIVERSITY   (Sweden)

Author keywords

Asp catalytic dyad; Aspartic proteases; BACE 1; HIV 1 PR; Ionizable residues; Low barrier hydrogen bonds; pH effect; Protonation states

Indexed keywords

4,7 DIBENZYL 2,3,4,5,6,7 HEXAHYDRO 5,6 DIHYDROXY 1,3 BIS[4 (HYDROXYMETHYL)BENZYL] 2H 1,3 DIAZEPIN 2 ONE; AMINO ACID; ASPARTIC PROTEINASE; ENZYME INHIBITOR; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; INDINAVIR; KYNOSTATIN 272; LIGAND; NELFINAVIR; PEPSTATIN; PEPTIDOMIMETIC AGENT; SAQUINAVIR;

BINDING AFFINITY; CATALYSIS; CHEMICAL STRUCTURE; DRUG DESIGN; HYDROGEN BOND; MOLECULAR MECHANICS; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTON TRANSPORT; REVIEW; X RAY CRYSTALLOGRAPHY;

ASPARTIC ACID PROTEASES; CATALYSIS; CATALYTIC DOMAIN; DRUG DESIGN; MODELS, MOLECULAR; PROTEASE INHIBITORS; PROTONS;

EID: 84878626336     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/1381612811319230009     Document Type: Review

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