6GVN

Tubulin:TM-3 DARPin complex

Summary for 6GVN

• Entry DOI: 10.2210/pdb6gvn/pdb
• Descriptor: Tubulin alpha chain, Tubulin beta chain, TM-3 DARPIN, ... (9 entities in total)
• Functional Keywords: microtubule, darpin, cell cycle
• Biological source: synthetic construct; More
• Total number of polymer chains: 3
• Total formula weight: 119823.20

Authors

Gigant, B.,Cantos Fernandes, S.,Campanacci, V. (deposition date: 2018-06-21, release date: 2019-04-24, Last modification date: 2024-01-17)

Primary citation

Campanacci, V.,Urvoas, A.,Cantos-Fernandes, S.,Aumont-Nicaise, M.,Arteni, A.A.,Velours, C.,Valerio-Lepiniec, M.,Dreier, B.,Pluckthun, A.,Pilon, A.,Pous, C.,Minard, P.,Gigant, B.
Insight into microtubule nucleation from tubulin-capping proteins.
Proc.Natl.Acad.Sci.USA, 116:9859-9864, 2019

PubMed Abstract: Nucleation is one of the least understood steps of microtubule dynamics. It is a kinetically unfavorable process that is templated in the cell by the γ-tubulin ring complex or by preexisting microtubules; it also occurs in vitro from pure tubulin. Here we study the nucleation inhibition potency of natural or artificial proteins in connection with their binding mode to the longitudinal surface of α- or β-tubulin. The structure of tubulin-bound CopN, a protein that delays nucleation, suggests that this protein may interfere with two protofilaments at the (+) end of a nucleus. Designed ankyrin repeat proteins that share a binding mode similar to that of CopN also impede nucleation, whereas those that target only one protofilament do not. In addition, an αRep protein predicted to target two protofilaments at the (-) end does not delay nucleation, pointing to different behaviors at both ends of the nucleus. Our results link the interference with protofilaments at the (+) end and the inhibition of nucleation.

PubMed: 31036638
DOI: 10.1073/pnas.1813559116

Experimental method

X-RAY DIFFRACTION (2.69 Å)