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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==
==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=''>
<StructureSection load='2l3l' size='340' side='right'caption='[[2l3l]]' scene=''>
== Structural highlights ==
== 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>
<table><tr><td colspan='2'>[[2l3l]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L3L FirstGlance]. <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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l3l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l3l RCSB], [http://www.ebi.ac.uk/pdbsum/2l3l PDBsum]</span><br>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l3l OCA], [https://pdbe.org/2l3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l3l RCSB], [https://www.ebi.ac.uk/pdbsum/2l3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l3l ProSAT]</span></td></tr>
== Publication Abstract from PubMed ==
</table>
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.
== Function ==
 
[https://www.uniprot.org/uniprot/TBCC_HUMAN TBCC_HUMAN] Tubulin-folding protein; involved in the final step of the tubulin folding pathway.<ref>PMID:11847227</ref>  
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>
 
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bruix, M.]]
[[Category: Large Structures]]
[[Category: Castano, R.]]
[[Category: Bruix M]]
[[Category: Garcia-Mayoral, M F.]]
[[Category: Castano R]]
[[Category: Lopez-Fanarraga, M L.]]
[[Category: Garcia-Mayoral MF]]
[[Category: Rico, M.]]
[[Category: Lopez-Fanarraga ML]]
[[Category: Zabala, J C.]]
[[Category: Rico M]]
[[Category: Chaperone]]
[[Category: Zabala JC]]
[[Category: Tubulin binding cofactor]]
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