5fnv: Difference between revisions

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<StructureSection load='5fnv' size='340' side='right'caption='[[5fnv]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
<StructureSection load='5fnv' size='340' side='right'caption='[[5fnv]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5fnv]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat], [http://en.wikipedia.org/wiki/Chick Chick] 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=5FNV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FNV FirstGlance]. <br>
<table><tr><td colspan='2'>[[5fnv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus], [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FNV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FNV FirstGlance]. <br>
</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=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>, <scene name='pdbligand=X3H:PIRONETIN'>X3H</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.61&#8491;</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=5fnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fnv OCA], [http://pdbe.org/5fnv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fnv RCSB], [http://www.ebi.ac.uk/pdbsum/5fnv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fnv ProSAT]</span></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=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>, <scene name='pdbligand=X3H:PIRONETIN'>X3H</scene></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=5fnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fnv OCA], [https://pdbe.org/5fnv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fnv RCSB], [https://www.ebi.ac.uk/pdbsum/5fnv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fnv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TBA1B_PIG 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. [[http://www.uniprot.org/uniprot/STMN4_RAT STMN4_RAT]] Exhibits microtubule-destabilizing activity.<ref>PMID:15039434</ref> <ref>PMID:12111843</ref> <ref>PMID:15014504</ref> [[http://www.uniprot.org/uniprot/TBB_PIG 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.
[https://www.uniprot.org/uniprot/STMN4_RAT STMN4_RAT] Exhibits microtubule-destabilizing activity.<ref>PMID:15039434</ref> <ref>PMID:12111843</ref> <ref>PMID:15014504</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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*[[Tubulin 3D Structures|Tubulin 3D Structures]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
*[[Tubulin tyrosine ligase|Tubulin tyrosine ligase]]
*[[Tubulin tyrosine ligase|Tubulin tyrosine ligase]]
*[[User:Alisa Cario|User:Alisa Cario]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Gallus gallus]]
[[Category: Chick]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Naismith, J]]
[[Category: Naismith J]]
[[Category: Wang, Y]]
[[Category: Wang Y]]
[[Category: Zhu, X]]
[[Category: Zhu X]]
[[Category: Structural protein]]
[[Category: Tubulin complex alpha-beta unsaturated lactone]]

Revision as of 10:00, 19 July 2023

a new complex structure of tubulin with an alpha-beta unsaturated lactonea new complex structure of tubulin with an alpha-beta unsaturated lactone

Structural highlights

5fnv is a 6 chain structure with sequence from Gallus gallus, Rattus norvegicus and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.61Å
Ligands:, , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

STMN4_RAT Exhibits microtubule-destabilizing activity.[1] [2] [3]

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.

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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

5fnv, resolution 2.61Å

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