2wfi | pdb_00002wfi
From Proteopedia
ATOMIC RESOLUTION CRYSTAL STRUCTURE OF THE PPIASE DOMAIN OF HUMAN CYCLOPHILIN G
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Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWater molecules doing time: Atomic-resolution crystal structures of the PPIase domain of cyclophilin G, alone and in complex with cyclosporin A, and together with MD simulations and calorimetry, reveal how trapped water molecules influence the thermodynamic profile of a protein-ligand interaction. The thermodynamic influence of trapped water molecules on a protein-ligand interaction.,Stegmann CM, Seeliger D, Sheldrick GM, de Groot BL, Wahl MC Angew Chem Int Ed Engl. 2009;48(28):5207-10. PMID:19499554[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 07:56, 29 September 2014.