4b1t

Structure of the factor Xa-like trypsin variant triple-Ala (TA) in complex with eglin C

spinqualitylabelsall models 4b1t, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4b1t is a 4 chain structure with sequence from Bos taurus and Hirudo medicinalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.78Å Ligands: CA, EDO, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRY1_BOVIN Publication Abstract from PubMed Abstract The energetics of macromolecular interactions are complex, particularly where protein flexibility is involved. Exploiting serendipitous differences in the plasticity of a series of closely related trypsin variants, we analyzed the enthalpic and entropic contributions accompanying interaction with L45K-eglin C. Binding of the four variants show significant differences in released heat, although the affinities vary little, in accordance with the principle of enthalpy-entropy compensation. Binding of the most disordered variant is almost entirely enthalpically driven, with practically no entropy change. As structures of the complexes reveal negligible differences in protein-inhibitor contacts, we conclude that solvent effects contribute significantly to binding affinities. Thermodynamic signatures in macromolecular interactions involving conformational flexibility.,Menzel A, Neumann P, Schwieger C, Stubbs MT Biol Chem. 2014 Jul 1;395(7-8):905-11. doi: 10.1515/hsz-2014-0177. PMID:25003391 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Eglin Trypsin 3D structures

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