5jqg

From Proteopedia

(Difference between revisions)

Revision as of 11:33, 17 June 2020

An apo tubulin-RB-TTL complex structure used for side-by-side comparison

Structural highlights

5jqg is a 6 chain structure with sequence from [1] and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , ,
Related:	5fnv
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TBA1B_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [STMN4_RAT] Exhibits microtubule-destabilizing activity.^[1] ^[2] ^[3] [TBB_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.

Publication Abstract from PubMed

Molecules that alter the normal dynamics of microtubule assembly and disassembly include many anticancer drugs in clinical use. So far all such therapeutics target beta-tubulin, and structural biology has explained the basis of their action and permitted design of new drugs. However, by shifting the profile of beta-tubulin isoforms, cancer cells become resistant to treatment. Compounds that bind to alpha-tubulin are less well characterized and unexploited. The natural product pironetin is known to bind to alpha-tubulin and is a potent inhibitor of microtubule polymerization. Previous reports had identified that pironetin reacts with lysine-352 residue however analogues designed on this model had much lower potency, which was difficult to explain, hindering further development. We report crystallographic and mass spectrometric data that reveal that pironetin forms a covalent bond to cysteine-316 in alpha-tubulin via a Michael addition reaction. These data provide a basis for the rational design of alpha-tubulin targeting chemotherapeutics.

Pironetin reacts covalently with cysteine-316 of alpha-tubulin to destabilize microtubule.,Yang J, Wang Y, Wang T, Jiang J, Botting CH, Liu H, Chen Q, Yang J, Naismith JH, Zhu X, Chen L Nat Commun. 2016 Jun 30;7:12103. doi: 10.1038/ncomms12103. PMID:27357539^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nakao C, Itoh TJ, Hotani H, Mori N. Modulation of the stathmin-like microtubule destabilizing activity of RB3, a neuron-specific member of the SCG10 family, by its N-terminal domain. J Biol Chem. 2004 May 28;279(22):23014-21. Epub 2004 Mar 22. PMID:15039434 doi:http://dx.doi.org/10.1074/jbc.M313693200
↑ Gavet O, El Messari S, Ozon S, Sobel A. Regulation and subcellular localization of the microtubule-destabilizing stathmin family phosphoproteins in cortical neurons. J Neurosci Res. 2002 Jun 1;68(5):535-50. PMID:12111843 doi:http://dx.doi.org/10.1002/jnr.10234
↑ Ravelli RB, Gigant B, Curmi PA, Jourdain I, Lachkar S, Sobel A, Knossow M. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature. 2004 Mar 11;428(6979):198-202. PMID:15014504 doi:http://dx.doi.org/10.1038/nature02393
↑ Yang J, Wang Y, Wang T, Jiang J, Botting CH, Liu H, Chen Q, Yang J, Naismith JH, Zhu X, Chen L. Pironetin reacts covalently with cysteine-316 of alpha-tubulin to destabilize microtubule. Nat Commun. 2016 Jun 30;7:12103. doi: 10.1038/ncomms12103. PMID:27357539 doi:http://dx.doi.org/10.1038/ncomms12103

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5jqg"

@@ Line 1: / Line 1: @@
 ==An apo tubulin-RB-TTL complex structure used for side-by-side comparison==
-<StructureSection load='5jqg' size='340' side='right' caption='[[5jqg]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
+<StructureSection load='5jqg' size='340' side='right'caption='[[5jqg]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5jqg]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JQG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5jqg]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JQG FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fnv|5fnv]]</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=5jqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqg OCA], [http://pdbe.org/5jqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jqg RCSB], [http://www.ebi.ac.uk/pdbsum/5jqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqg ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqg OCA], [http://pdbe.org/5jqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jqg RCSB], [http://www.ebi.ac.uk/pdbsum/5jqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqg ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5jqg" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Stathmin-4 3D structures|Stathmin-4 3D structures]]
+*[[Tubulin 3D Structures|Tubulin 3D Structures]]
+*[[Tubulin tyrosine ligase|Tubulin tyrosine ligase]]
+*[[User:Alisa Cario|User:Alisa Cario]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Sus scrofa]]
 [[Category: Naismith, J H]]

5jqg

From Proteopedia

Revision as of 11:33, 17 June 2020

An apo tubulin-RB-TTL complex structure used for side-by-side comparison

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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