2l3l | pdb_00002l3l

The solution structure of the N-terminal domain of human Tubulin Binding Cofactor C reveals a platform for the interaction with ab-tubulin

spinqualitylabelsall models 2l3l, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l3l is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Human Tubulin Binding Cofactor C (hTBCC) is a 346 amino acid protein composed of two domains, which is involved in the folding pathway of newly synthesized alpha and beta-tubulins. The 3D structure of the 111-residue hTBCC N-terminal domain of the protein has not yet been determined. As a previous step to that end, here we report the NMR (1)H, (15)N, and (13)C chemical shift assignments at pH 6.0 and 25 degrees C, based on a uniformly doubly labelled (13)C/(15)N sample of the domain. 1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Binding Cofactor C.,Garcia-Mayoral MF, Castano R, Zabala JC, Santoro J, Rico M, Bruix M Biomol NMR Assign. 2010 Oct;4(2):219-21. Epub 2010 Jul 9. PMID:20617401 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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