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Bioorganic and Medicinal Chemistry Letters

Volumn 25, Issue 7, 2015, Pages 1385-1389

The zinc coordination pattern in the η-carbonic anhydrase from Plasmodium falciparum is different from all other carbonic anhydrase genetic families

(4) De Simone, Giuseppina a Di Fiore, Anna a Capasso, Clemente b Supuran, Claudiu T c

a CNR (Italy)

b CNR (Italy)

c UNIVERSITY OF FLORENCE (Italy)

Author keywords

Carbonic anhydrase; Homology modeling; Plasmodium falciparum; Zinc coordination; Class; Class

Indexed keywords

BACTERIAL ENZYME; CARBONATE DEHYDRATASE; ETA CARBONATE DEHYDRATASE; HISTIDINE; NUCLEOPHILE; UNCLASSIFIED DRUG; ZINC COMPLEX; CARBONATE DEHYDRATASE INHIBITOR; ZINC;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; DRUG DESIGN; GEOMETRY; HYDRATION; INDEL MUTATION; NONHUMAN; PH; PLASMODIUM FALCIPARUM; PROTEIN DOMAIN; PROTEIN MOTIF; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; STRUCTURE ACTIVITY RELATION; SYNTHESIS; X RAY CRYSTALLOGRAPHY;

CARBONIC ANHYDRASE INHIBITORS; CARBONIC ANHYDRASES; CRYSTALLOGRAPHY, X-RAY; DRUG DESIGN; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PLASMODIUM FALCIPARUM; STRUCTURE-ACTIVITY RELATIONSHIP; ZINC;

EID: 84925498524 PISSN: 0960894X EISSN: 14643405 Source Type: Journal
DOI: 10.1016/j.bmcl.2015.02.046 Document Type: Article

Times cited : (115)

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