2l3l - Revision history

OCA at 06:52, 1 May 2024

2024-05-01T06:52:23Z

←Older revision		Revision as of 06:52, 1 May 2024
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	== Structural highlights ==		== Structural highlights ==
	<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>		<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>
-	</td></tr><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>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
		+	<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>
	</table>		</table>
	== Function ==		== 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>		[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>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Human Tubulin Binding Cofactor C (TBCC) is a post-chaperonin involved in the folding and assembly of alpha- and beta-tubulin monomers leading to the release of productive tubulin heterodimers ready to polymerize into microtubules. In this process it collaborates with other cofactors (TBC's A, B, D, and E) and forms a supercomplex with TBCD, beta-tubulin, TBCE and alpha-tubulin. Here, we demonstrate that TBCC depletion results in multipolar spindles and mitotic failure. Accordingly, TBCC is found at the centrosome and is implicated in bipolar spindle formation. We also determine by NMR the structure of the N-terminal domain of TBCC. The TBCC N-terminal domain adopts a spectrin-like fold topology composed of a left-handed 3-stranded alpha-helix bundle. Remarkably, the 30-residue N-terminal segment of the TBCC N-terminal domain is flexible and disordered in solution. This unstructured region is involved in the interaction with tubulin. Our data lead us to propose a testable model for TBCC N-terminal domain/tubulin recognition in which the highly charged N-terminus as well as residues from the three helices and the loops interact with the acidic hypervariable regions of tubulin monomers.
-
-	The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.,Garcia-Mayoral MF, Castano R, Fanarraga ML, Zabala JC, Rico M, Bruix M PLoS One. 2011;6(10):e25912. doi: 10.1371/journal.pone.0025912. Epub 2011 Oct 18. PMID:22028797<ref>PMID:22028797</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2l3l" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:15, 18 January 2023

2023-01-18T08:15:52Z

←Older revision		Revision as of 08:15, 18 January 2023
Line 1:		Line 1:

	==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 ==
-	<table><tr><td colspan='2'>[[2l3l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. 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>	+	<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>
-	</td></tr>~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TBCC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+	</td></tr><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>
-	<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>	+
	</table>		</table>
	== Function ==		== 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>	+	[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== 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~~.	+	Human Tubulin Binding Cofactor C (TBCC) is a post-chaperonin involved in the folding and assembly of alpha- and beta-tubulin monomers leading to the release of productive tubulin heterodimers ready to polymerize into microtubules. In this process it collaborates with other cofactors (TBC's A, B, D, and E) and forms a supercomplex with TBCD, beta-tubulin, TBCE and alpha-tubulin. Here, we demonstrate that TBCC depletion results in multipolar spindles and mitotic failure. Accordingly, TBCC is found at the centrosome and is implicated in bipolar spindle formation. We also determine by NMR the structure of the N-terminal domain of TBCC. The TBCC N-terminal domain adopts a spectrin-like fold topology composed of a left-handed 3-stranded alpha-helix bundle. Remarkably, the 30-residue N-terminal segment of the TBCC N-terminal domain is flexible and disordered in solution. This unstructured region is involved in the interaction with tubulin. Our data lead us to propose a testable model for TBCC N-terminal domain/tubulin recognition in which the highly charged N-terminus as well as residues from the three helices and the loops interact with the acidic hypervariable regions of tubulin monomers.

-	~~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>	+	The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.,Garcia-Mayoral MF, Castano R, Fanarraga ML, Zabala JC, Rico M, Bruix M PLoS One. 2011;6(10):e25912. doi: 10.1371/journal.pone.0025912. Epub 2011 Oct 18. PMID:22028797<ref>PMID:22028797</ref>

	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
Line 22:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bruix, M]]	+	[[Category: Bruix M]]
-	[[Category: Castano, R]]	+	[[Category: Castano R]]
-	[[Category: Garcia-Mayoral~~, M F~~]]	+	[[Category: Garcia-Mayoral MF]]
-	[[Category: Lopez-Fanarraga~~, M L~~]]	+	[[Category: Lopez-Fanarraga ML]]
-	[[Category: Rico, M]]	+	[[Category: Rico M]]
-	[[Category: Zabala~~, J C]]~~	+	[[Category: Zabala JC]]
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Tubulin binding cofactor~~]]	+

OCA at 07:35, 14 April 2021

2021-04-14T07:35:49Z

←Older revision		Revision as of 07:35, 14 April 2021
Line 1:		Line 1:

	==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]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2l3l]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. 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 [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2L3L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2l3l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TBCC ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TBCC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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~~://pdbe.org/2l3l PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2l3l RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2l3l PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2l3l ProSAT]</span></td></tr>	+	<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>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://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>	+	[[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bruix, M]]		[[Category: Bruix, M]]
	[[Category: Castano, R]]		[[Category: Castano, R]]

OCA at 08:21, 25 July 2018

2018-07-25T08:21:17Z

←Older revision		Revision as of 08:21, 25 July 2018
Line 1:		Line 1:
		+
	==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]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[2l3l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L3L FirstGlance]. <br>		<table><tr><td colspan='2'>[[2l3l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L3L FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TBCC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TBCC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2l3l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l3l RCSB], [http://www.ebi.ac.uk/pdbsum/2l3l PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2l3l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l3l RCSB], [http://www.ebi.ac.uk/pdbsum/2l3l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l3l ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 19:32, 10 September 2015

2015-09-10T19:32:16Z

←Older revision		Revision as of 19:32, 10 September 2015
Line 2:		Line 2:
	<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]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L3L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2l3l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L3L FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TBCC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TBCC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2l3l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l3l RCSB], [http://www.ebi.ac.uk/pdbsum/2l3l PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 16:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2l3l" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Bruix, M]]		[[Category: Bruix, M]]
	[[Category: Castano, R]]		[[Category: Castano, R]]

OCA at 05:03, 25 December 2014

2014-12-25T05:03:48Z

←Older revision		Revision as of 05:03, 25 December 2014
Line 6:		Line 6:
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 05:46, 22 December 2014

2014-12-22T05:46:49Z

←Older revision		Revision as of 05:46, 22 December 2014
Line 2:		Line 2:
	<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]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[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 [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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L3L FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TBCC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TBCC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr~~><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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></td></tr>
-	~~<tr~~><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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></td></tr>	+	</table>
-	<table>	+
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 13:		Line 12:
	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>		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 ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
	== References ==		== References ==
Line 20:		Line 19:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Bruix, M.]]	+	[[Category: Bruix, M]]
-	[[Category: Castano, R.]]	+	[[Category: Castano, R]]
-	[[Category: Garcia-Mayoral, M F.]]	+	[[Category: Garcia-Mayoral, M F]]
-	[[Category: Lopez-Fanarraga, M L.]]	+	[[Category: Lopez-Fanarraga, M L]]
-	[[Category: Rico, M.]]	+	[[Category: Rico, M]]
-	[[Category: Zabala, J C.]]	+	[[Category: Zabala, J C]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
	[[Category: Tubulin binding cofactor]]		[[Category: Tubulin binding cofactor]]

OCA at 09:46, 1 May 2014

2014-05-01T09:46:59Z

←Older revision		Revision as of 09:46, 1 May 2014
Line 2:		Line 2:
	<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]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' 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 [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>	+	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TBCC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== 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.		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.
Line 11:		Line 14:

	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:09, 30 April 2014

2014-04-30T10:09:26Z

←Older revision		Revision as of 10:09, 30 April 2014
Line 4:		Line 4:
	[[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>		[[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>		<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>
		+	<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>
	== Publication Abstract from PubMed ==		== 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.		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.

OCA at 08:30, 30 April 2014

2014-04-30T08:30:30Z

←Older revision		Revision as of 08:30, 30 April 2014
Line 1:		Line 1:
-	[[~~Image:~~2l3l~~.jpg~~\|~~left\|200px~~]]	+	==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>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_2l3l"~~, ~~creates the "Structure Box" on the page~~.	+
-	~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display~~.	+
-	-->	+
-	~~{{STRUCTURE_2l3l\| PDB=2l3l \| SCENE= }}~~	+

-	~~===The solution structure~~ of the ~~N-terminal domain of human Tubulin Binding Cofactor C reveals a platform for the interaction with ab-tubulin===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	== References ==
-		+	<references/>
-	~~<!--~~	+	__TOC__
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_20617401}}, adds the Publication Abstract to the page~~	+	</StructureSection>
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 20617401 is the PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_20617401}}~~	+
-		+
-	==~~About this Structure~~==	+
-	~~[[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].~~	+
-		+
-	~~==Reference==~~	+
-	<~~ref group="xtra">PMID:020617401</ref><references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bruix, M.]]		[[Category: Bruix, M.]]