 |
PDBsum entry 6gwc
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
431 a.a.
|
|
|
|
|
|
|
|
|
|
|
417 a.a.
|
|
|
|
|
|
|
|
|
|
|
217 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Selection and characterization of artificial proteins targeting the tubulin α subunit.
|
|
|
Authors
|
|
V.Campanacci,
A.Urvoas,
T.Consolati,
S.Cantos-Fernandes,
M.Aumont-Nicaise,
M.Valerio-Lepiniec,
T.Surrey,
P.Minard,
B.Gigant.
|
|
|
Ref.
|
|
Structure, 2019,
27,
497.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Microtubules are cytoskeletal filaments of eukaryotic cells made of αβ-tubulin
heterodimers. Structural studies of non-microtubular tubulin rely mainly on
molecules that prevent its self-assembly and are used as crystallization
chaperones. Here we identified artificial proteins from an αRep library that
are specific to α-tubulin. Turbidity experiments indicate that these αReps
impede microtubule assembly in a dose-dependent manner and total internal
reflection fluorescence microscopy further shows that they specifically block
growth at the microtubule (-) end. Structural data indicate that they do so by
targeting the α-tubulin longitudinal surface. Interestingly, in one of the
complexes studied, the α subunit is in a conformation that is intermediate
between the ones most commonly observed in X-ray structures of tubulin and those
seen in the microtubule, emphasizing the plasticity of tubulin. These
α-tubulin-specific αReps broaden the range of tools available for the
mechanistic study of microtubule dynamics and its regulation.
|
|
|
|
|
|
|
