Crystal structure of human soluble adenylate cyclase reveals a distinct, highly flexible allosteric bicarbonate binding pocket

ChemMedChem

Volumn 9, Issue 4, 2014, Pages 823-832

  Saalau Bethell, Susanne M ^a   Berdini, Valerio ^a   Cleasby, Anne ^a   Congreve, Miles ^a,b   Coyle, Joseph E ^a   Lock, Victoria ^a,c   Murray, Christopher W ^a   O'Brien, M Alistair ^a,b   Rich, Sharna J ^a   Sambrook, Tracey ^a,d   Vinkovic, Mladen ^a   Yon, Jeff R ^a   Jhoti, Harren ^a  

^a ASTEX PHARMACEUTICALS   (United Kingdom)

^b Heptares Therapeutics Ltd   (United Kingdom)

^c Gregory Fryer Associates Ltd   (United Kingdom)

^d Stem Cell Sciences UK Ltd   (United Kingdom)

Author keywords

allosterism; drug discovery; enzyme regulation; fragment screening; structural biology

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DERIVATIVE; ADENYLATE CYCLASE; ADENYLATE CYCLASE INHIBITOR; ALPHA,BETA METHYLENE ADENOSINE 5' TRIPHOSPHATE; APOPROTEIN; BICARBONATE; CALCIUM; UNCLASSIFIED DRUG; ADCY10 PROTEIN, HUMAN; ENZYME INHIBITOR;

ALLOSTERISM; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CYCLIZATION; DRUG POTENCY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; LIGAND BINDING; PRIORITY JOURNAL; SECOND MESSENGER; SYNTHESIS; ANTAGONISTS AND INHIBITORS; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; DRUG EFFECTS; HUMAN; METABOLISM; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ADENYLATE CYCLASE; BICARBONATES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME ACTIVATION; ENZYME INHIBITORS; HUMANS; MODELS, MOLECULAR; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84897993705     PISSN: 18607179     EISSN: 18607187     Source Type: Journal    
DOI: 10.1002/cmdc.201300480     Document Type: Article

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