1sa0
From Proteopedia
(New page: 200px<br /><applet load="1sa0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sa0, resolution 3.58Å" /> '''TUBULIN-COLCHICINE: ...) |
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| - | [[Image:1sa0.gif|left|200px]]<br /><applet load="1sa0" size=" | + | [[Image:1sa0.gif|left|200px]]<br /><applet load="1sa0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sa0, resolution 3.58Å" /> | caption="1sa0, resolution 3.58Å" /> | ||
'''TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX'''<br /> | '''TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Microtubules are cytoskeletal polymers of tubulin involved in many | + | Microtubules are cytoskeletal polymers of tubulin involved in many cellular functions. Their dynamic instability is controlled by numerous compounds and proteins, including colchicine and stathmin family proteins. The way in which microtubule instability is regulated at the molecular level has remained elusive, mainly because of the lack of appropriate structural data. Here, we present the structure, at 3.5 A resolution, of tubulin in complex with colchicine and with the stathmin-like domain (SLD) of RB3. It shows the interaction of RB3-SLD with two tubulin heterodimers in a curved complex capped by the SLD amino-terminal domain, which prevents the incorporation of the complexed tubulin into microtubules. A comparison with the structure of tubulin in protofilaments shows changes in the subunits of tubulin as it switches from its straight conformation to a curved one. These changes correlate with the loss of lateral contacts and provide a rationale for the rapid microtubule depolymerization characteristic of dynamic instability. Moreover, the tubulin-colchicine complex sheds light on the mechanism of colchicine's activity: we show that colchicine binds at a location where it prevents curved tubulin from adopting a straight structure, which inhibits assembly. |
==About this Structure== | ==About this Structure== | ||
| - | 1SA0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG, GTP, GDP and CN2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1SA0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GTP:'>GTP</scene>, <scene name='pdbligand=GDP:'>GDP</scene> and <scene name='pdbligand=CN2:'>CN2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SA0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Curmi, P | + | [[Category: Curmi, P A.]] |
[[Category: Gigant, B.]] | [[Category: Gigant, B.]] | ||
[[Category: Jourdain, I.]] | [[Category: Jourdain, I.]] | ||
[[Category: Knossow, M.]] | [[Category: Knossow, M.]] | ||
[[Category: Lachkar, S.]] | [[Category: Lachkar, S.]] | ||
| - | [[Category: Ravelli, R | + | [[Category: Ravelli, R B.]] |
[[Category: Sobel, A.]] | [[Category: Sobel, A.]] | ||
[[Category: CN2]] | [[Category: CN2]] | ||
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[[Category: tubulin]] | [[Category: tubulin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:24 2008'' |
Revision as of 12:59, 21 February 2008
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TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX
Overview
Microtubules are cytoskeletal polymers of tubulin involved in many cellular functions. Their dynamic instability is controlled by numerous compounds and proteins, including colchicine and stathmin family proteins. The way in which microtubule instability is regulated at the molecular level has remained elusive, mainly because of the lack of appropriate structural data. Here, we present the structure, at 3.5 A resolution, of tubulin in complex with colchicine and with the stathmin-like domain (SLD) of RB3. It shows the interaction of RB3-SLD with two tubulin heterodimers in a curved complex capped by the SLD amino-terminal domain, which prevents the incorporation of the complexed tubulin into microtubules. A comparison with the structure of tubulin in protofilaments shows changes in the subunits of tubulin as it switches from its straight conformation to a curved one. These changes correlate with the loss of lateral contacts and provide a rationale for the rapid microtubule depolymerization characteristic of dynamic instability. Moreover, the tubulin-colchicine complex sheds light on the mechanism of colchicine's activity: we show that colchicine binds at a location where it prevents curved tubulin from adopting a straight structure, which inhibits assembly.
About this Structure
1SA0 is a Protein complex structure of sequences from Bos taurus and Rattus norvegicus with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain., Ravelli RB, Gigant B, Curmi PA, Jourdain I, Lachkar S, Sobel A, Knossow M, Nature. 2004 Mar 11;428(6979):198-202. PMID:15014504
Page seeded by OCA on Thu Feb 21 14:59:24 2008
Categories: Bos taurus | Protein complex | Rattus norvegicus | Curmi, P A. | Gigant, B. | Jourdain, I. | Knossow, M. | Lachkar, S. | Ravelli, R B. | Sobel, A. | CN2 | GDP | GTP | MG | Alpha-tubulin | Beta-tubulin | Colchicine | Gtpase | Microtubule podophyllotoxin | Stathmin | Tubulin
