4o2b

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m (Protected "4o2b" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4o2b| PDB=4o2b | SCENE= }}
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===Tubulin-Colchicine complex===
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{{ABSTRACT_PUBMED_24530796}}
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The entry 4o2b is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/TBA1B_BOVIN TBA1B_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. [[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).
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Authors: Prota, A.E., Franck, D., Bachmann, F., Bargsten, K., Buey, R.M., Pohlmann, J., Reinelt, S., Lane, H., Steinmetz, M.O.
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==About this Structure==
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[[4o2b]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O2B OCA].
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Description: Tubulin-Colchicine complex
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==Reference==
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<ref group="xtra">PMID:024530796</ref><references group="xtra"/><references/>
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[[Category: Bos taurus]]
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[[Category: Buffalo rat]]
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[[Category: Chick]]
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[[Category: Bachmann, F.]]
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[[Category: Bargsten, K.]]
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[[Category: Buey, R M.]]
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[[Category: Franck, D.]]
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[[Category: Lane, H.]]
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[[Category: Pohlmann, J.]]
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[[Category: Prota, A E.]]
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[[Category: Reinelt, S.]]
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[[Category: Steinmetz, M O.]]
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[[Category: Alpha-tubulin]]
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[[Category: Beta-tubulin]]
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[[Category: Cell cycle]]
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[[Category: Cell cycle-inhibitor complex]]
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[[Category: Colchicine]]
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[[Category: Cytoskeleton]]
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[[Category: Gtpase]]
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[[Category: Ligase]]
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[[Category: Microtubule]]
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[[Category: Stathmin]]
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[[Category: Tubulin fold]]

Revision as of 08:12, 16 April 2014

Template:STRUCTURE 4o2b

Contents

Tubulin-Colchicine complex

Template:ABSTRACT PUBMED 24530796

Function

[TBA1B_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. [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).

About this Structure

4o2b is a 6 chain structure with sequence from Bos taurus, Buffalo rat and Chick. Full crystallographic information is available from OCA.

Reference

  • Prota AE, Danel F, Bachmann F, Bargsten K, Buey RM, Pohlmann J, Reinelt S, Lane H, Steinmetz MO. The Novel Microtubule-Destabilizing Drug BAL27862 Binds to the Colchicine Site of Tubulin with Distinct Effects on Microtubule Organization. J Mol Biol. 2014 Apr 17;426(8):1848-60. doi: 10.1016/j.jmb.2014.02.005. Epub 2014, Feb 11. PMID:24530796 doi:http://dx.doi.org/10.1016/j.jmb.2014.02.005
  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

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