Kinetics, in silico docking, molecular dynamics, and MM-GBSA binding studies on prototype indirubins, KT5720, and staurosporine as phosphorylase kinase ATP-binding site inhibitors: The role of water molecules examined

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 3, 2011, Pages 703-719

  Hayes, Joseph M ^a   Skamnaki, Vicky T ^a,b   Archontis, Georgios ^c   Lamprakis, Christos ^a   Sarrou, Josephine ^a   Bischler, Nicolas ^a   Skaltsounis, Alexios Leandros ^d   Zographos, Spyros E ^a   Oikonomakos, Nikos G ^a  

^a INSTITUTE OF BIOLOGY   (Greece)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF CYPRUS   (Cyprus)

^d UNIVERSITY OF ATHENS   (Greece)

Author keywords

Desmond molecular dynamics; Induced fit docking; Protein kinase inhibitors; Receptor flexibility; Type 2 diabetes

Indexed keywords

ADENINE; ADENOSINE TRIPHOSPHATE; INDIRUBIN; INDIRUBIN 3' OXIME; KT 5720; PHOSPHORYLASE KINASE; STAUROSPORINE; UNCLASSIFIED DRUG; WATER;

ARTICLE; DRUG STRUCTURE; GLYCOGENOLYSIS; HYDROGEN BOND; IC 50; MOLECULAR DOCKING; NON INSULIN DEPENDENT DIABETES MELLITUS; PRIORITY JOURNAL; PROTEIN BINDING; SEQUENCE HOMOLOGY; STATIC ELECTRICITY;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BASE SEQUENCE; CARBAZOLES; DNA PRIMERS; INDOLES; KINETICS; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; PHOSPHORYLASE KINASE; PYRROLES; SEQUENCE HOMOLOGY, AMINO ACID; STAUROSPORINE; WATER;

EID: 79551492697     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22890     Document Type: Article

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