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427 a.a.
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419 a.a.
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124 a.a.
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* Residue conservation analysis
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PDB id:
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Cell cycle
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Title:
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Tubulin-colchicine-soblidotin: stathmin-like domain complex
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Structure:
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Tubulin alpha-1c chain. Chain: a, c. Synonym: tubulin alpha chain. Tubulin beta-2b chain. Chain: b, d. Synonym: tubulin beta chain. Stathmin-4. Chain: e. Fragment: rb3 stathmin-like domain 4.
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Source:
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Bos taurus. Bovine. Organism_taxid: 9913. Organ: brain. Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: stmn4. Expressed in: escherichia coli.
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Resolution:
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3.80Å
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R-factor:
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0.231
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R-free:
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0.295
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Authors:
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A.Cormier,M.Marchand,R.B.Ravelli,M.Knossow,B.Gigant
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Key ref:
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A.Cormier
et al.
(2008).
Structural insight into the inhibition of tubulin by vinca domain peptide ligands.
Embo Rep,
9,
1101-1106.
PubMed id:
DOI:
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Date:
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05-Aug-08
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Release date:
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21-Oct-08
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PROCHECK
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Headers
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References
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Q3ZCJ7
(TBA1C_BOVIN) -
Tubulin alpha-1C chain
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Seq:
Struc:
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449 a.a.
427 a.a.
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Gene Ontology (GO) functional annotation
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Cellular component
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protein complex
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4 terms
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Biological process
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intracellular signal transduction
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6 terms
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Biochemical function
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structural molecule activity
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4 terms
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DOI no:
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Embo Rep
9:1101-1106
(2008)
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PubMed id:
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Structural insight into the inhibition of tubulin by vinca domain peptide ligands.
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A.Cormier,
M.Marchand,
R.B.Ravelli,
M.Knossow,
B.Gigant.
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ABSTRACT
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The tubulin vinca domain is the target of widely different microtubule
inhibitors that interfere with the binding of vinblastine. Although all these
ligands inhibit the hydrolysis of GTP, they affect nucleotide exchange to
variable extents. The structures of two vinca domain antimitotic
peptides--phomopsin A and soblidotin (a dolastatin 10 analogue)--bound to
tubulin in a complex with a stathmin-like domain show that their sites partly
overlap with that of vinblastine and extend the definition of the vinca domain.
The structural data, together with the biochemical results from the ligands we
studied, highlight two main contributors in nucleotide exchange: the flexibility
of the tubulin subunits' arrangement at their interfaces and the residues in the
carboxy-terminal part of the beta-tubulin H6-H7 loop. The structures also
highlight common features of the mechanisms by which vinca domain ligands favour
curved tubulin assemblies and destabilize microtubules.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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R.A.Stanton,
K.M.Gernert,
J.H.Nettles,
and
R.Aneja
(2011).
Drugs that target dynamic microtubules: a new molecular perspective.
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Med Res Rev, 31,
443-481.
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C.Dumontet,
and
M.A.Jordan
(2010).
Microtubule-binding agents: a dynamic field of cancer therapeutics.
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Nat Rev Drug Discov, 9,
790-803.
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D.Calligaris,
P.Verdier-Pinard,
F.Devred,
C.Villard,
D.Braguer,
and
D.Lafitte
(2010).
Microtubule targeting agents: from biophysics to proteomics.
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Cell Mol Life Sci, 67,
1089-1104.
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J.A.Smith,
L.Wilson,
O.Azarenko,
X.Zhu,
B.M.Lewis,
B.A.Littlefield,
and
M.A.Jordan
(2010).
Eribulin binds at microtubule ends to a single site on tubulin to suppress dynamic instability.
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Biochemistry, 49,
1331-1337.
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A.Cormier,
M.J.Clément,
M.Knossow,
S.Lachkar,
P.Savarin,
F.Toma,
A.Sobel,
B.Gigant,
and
P.A.Curmi
(2009).
The PN2-3 domain of centrosomal P4.1-associated protein implements a novel mechanism for tubulin sequestration.
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J Biol Chem, 284,
6909-6917.
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A.Dorléans,
B.Gigant,
R.B.Ravelli,
P.Mailliet,
V.Mikol,
and
M.Knossow
(2009).
Variations in the colchicine-binding domain provide insight into the structural switch of tubulin.
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Proc Natl Acad Sci U S A, 106,
13775-13779.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
