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2l3l
From Proteopedia
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| - | [[ | + | ==The solution structure of the N-terminal domain of human Tubulin Binding Cofactor C reveals a platform for the interaction with ab-tubulin== |
| + | <StructureSection load='2l3l' size='340' side='right' caption='[[2l3l]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | [[2l3l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L3L OCA]. <br> | ||
| + | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | ||
| + | == 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<ref>PMID:20617401</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Bruix, M.]] | [[Category: Bruix, M.]] | ||
Revision as of 08:30, 30 April 2014
The solution structure of the N-terminal domain of human Tubulin Binding Cofactor C reveals a platform for the interaction with ab-tubulin
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