Do crystal structures obviate the need for theoretical models of GPCRs for structure-based virtual screening?

Proteins: Structure, Function and Bioinformatics

Volumn 80, Issue 6, 2012, Pages 1503-1521

  Tang, Hao ^a,b   Wang, Xiang Simon ^c   Hsieh, Jui Hua ^a   Tropsha, Alexander ^a  

^a UNIVERSITY OF NORTH CAROLINA   (United States)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^c HOWARD UNIVERSITY   (United States)

Author keywords

Agonist bound; Antagonist bound; molecular docking; Beta 2 adrenoreceptor; Crystallography; Enrichment factor; GPCRs modeling

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR BLOCKING AGENT; BETA 2 ADRENERGIC RECEPTOR STIMULATING AGENT; G PROTEIN COUPLED RECEPTOR; LIGAND;

ACCURACY; ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; DRUG SCREENING; MOLECULAR STABILITY; PRIORITY JOURNAL; PROTEIN INTERACTION; SCREENING; THEORETICAL MODEL; X RAY CRYSTALLOGRAPHY;

ADRENERGIC BETA-2 RECEPTOR AGONISTS; ADRENERGIC BETA-2 RECEPTOR ANTAGONISTS; AMINO ACID SEQUENCE; BINDING SITES; CLUSTER ANALYSIS; COMPUTATIONAL BIOLOGY; CRYSTALLOGRAPHY, X-RAY; DRUG DISCOVERY; HUMANS; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; RECEPTORS, ADRENERGIC, BETA-2; RECEPTORS, G-PROTEIN-COUPLED; ROC CURVE; SEQUENCE ALIGNMENT;

EID: 84862789167     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24035     Document Type: Article

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