5zxh: Difference between revisions

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'''Unreleased structure'''


The entry 5zxh is ON HOLD  until Paper Publication
==The structure of MT189-tubulin complex==
 
<StructureSection load='5zxh' size='340' side='right'caption='[[5zxh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
Authors: Li, Z.P., Wang, Y.X., Meng, T., Yang, J.L., Chen, Q.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5zxh]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZXH FirstGlance]. <br>
Description: The structure of MT189-tubulin complex
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9LX:2-(6-fluoro-3-{[(4-methoxyphenyl)methyl]amino}imidazo[1,2-a]pyridin-2-yl)phenol'>9LX</scene>, <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></td></tr>
[[Category: Unreleased Structures]]
<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=5zxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zxh OCA], [http://pdbe.org/5zxh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zxh RCSB], [http://www.ebi.ac.uk/pdbsum/5zxh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zxh ProSAT]</span></td></tr>
[[Category: Wang, Y.X]]
</table>
== 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/TBB2B_BOVIN TBB2B_BOVIN]] 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 (By similarity).
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Chen, Q]]
[[Category: Li, Z P]]
[[Category: Meng, T]]
[[Category: Meng, T]]
[[Category: Li, Z.P]]
[[Category: Wang, Y X]]
[[Category: Chen, Q]]
[[Category: Yang, J L]]
[[Category: Yang, J.L]]
[[Category: Structural protein]]
[[Category: Tubulin complex]]

Revision as of 09:42, 23 May 2019

The structure of MT189-tubulin complexThe structure of MT189-tubulin complex

Structural highlights

5zxh is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , , ,
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] [TBB2B_BOVIN] 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 (By similarity).

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

5zxh, resolution 2.80Å

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