7q0x | pdb_00007q0x

Bovine Trypsin co-crystallized with V(IV)OSO4 and pic

spinqualitylabelsall models 7q0x, resolution 1.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7q0x is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 6PC, CA, GOL, O, SO4, V Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TRY1_BOVIN] Publication Abstract from PubMed Vanadium compounds have frequently been proposed as therapeutics, but their application has been hampered by the lack of information on the different V-containing species that may form and how these interact with blood and cell proteins, and with enzymes. Herein, we report several resolved crystal structures of lysozyme with bound V(IV) O(2+) and V(IV) OL(2+) , where L=2,2'-bipyridine or 1,10-phenanthroline (phen), and of trypsin with V(IV) O(picolinato)2 and V(V) O2 (phen)(+) moieties. Computational studies complete the refinement and shed light on the relevant role of hydrophobic interactions, hydrogen bonds, and microsolvation in stabilizating the structure. Noteworthy is that the trypsin-V(V) O2 (phen) and trypsin-V(IV) O(OH)(phen) adducts correspond to similar energies, thus suggesting a possible interconversion under physiological/biological conditions. The obtained data support the relevance of hydrolysis of V(IV) and V(V) complexes in the several types of binding established with proteins and the formation of different adducts that might contribute to their pharmacological action, and significantly widen our knowledge of vanadium-protein interactions. Binding of V(IV) O(2+) , V(IV) OL, V(IV) OL2 and V(V) O2 L Moieties to Proteins: X-ray/Theoretical Characterization and Biological Implications.,Santos MFA, Sciortino G, Correia I, Fernandes ACP, Santos-Silva T, Pisanu F, Garribba E, Costa Pessoa J Chemistry. 2022 Apr 29:e202200105. doi: 10.1002/chem.202200105. PMID:35486702 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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