3ly6 | pdb_00003ly6

Crystal structure of human transglutaminase 2 complex with adenosine 5' Triphosphate

spinqualitylabelsall models 3ly6, resolution 3.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ly6 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.14Å Ligands: ATP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TGM2_HUMAN Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. 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 PubMed Transglutaminase 2 (TG2) is a calcium-dependent multifunctional protein associated with various human diseases. We determined the crystal structure of human TG2 in complex with adenosine triphosphate (ATP). The ATP molecule binds to the previously identified guanosine diphosphate (GDP) binding pocket but has different hydrogen bonds and ion interaction with protein. The four residues Arg476, Arg478, Val479 and Tyr583, all of which are involved in both ATP and GDP binding by hydrogen bonds, might play important roles in the stabilization of TG2 by ATP or GDP. However, Ser482 and Arg580, which are involved in GDP binding, do not form hydrogen bond with ATP. Additionally, we newly discovered an intramolecular disulfide bond between Cys230 and Cys370, which formation might regulate the enzymatic activity of TG2. Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate.,Han BG, Cho JW, Cho YD, Jeong KC, Kim SY, Lee BI Int J Biol Macromol. 2010 Aug 1;47(2):190-5. Epub 2010 May 5. PMID:20450932 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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