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Table 11.1
Accession numbers for structures of human (*) or mouse (**) tubulin-
specific chaperones in the PDB database ( http://www.rcsb.org/pdb/home/home.do )
TBCA*
Whole molecule
1H7C
TBCB**
N-terminal Ubl-domain
1V6E
TBCB**
C-terminal CAP-Gly domain
1WHG
TBCC*
N-terminal domain
2L3L
TBCC*
C-terminal domain
2YUH
TBCE**
C-terminal Ubl-domain
1WJN
with microtubule plus ends or indirectly via other
TIPs. No clear evidence for such
interactions currently exists, but this may reflect equilibriumdissociation constants that
are too weak for the formation of stable complexes.
The ability to generate tubulin-specific chaperones as recombinant proteins
has been essential for the acquisition of structural data ( Table 11.1 ), although
(with the exception of TBCA) this information is incomplete in the sense that it is cur-
rently limited to individual domains, and there is as yet no structural data on TBCD.
Nonetheless, the available structures represent an important step toward a mechanistic
understanding of the molecular machinery that assembles the a / b heterodimer.
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References
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