Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes

Autor: Yiu Wing Sunny Cheung, Thiago V. Seraphim, Carlos H.I. Ramos, Gavin Young, Júlio César Borges, Lisandra M. Gava, Yu-Qian Mao, Leandro R.S. Barbosa, Daniel R. Southworth, Mohan Babu, Siripat Aluksanasuwan, Visith Thongboonkerd, Carol V. Robinson, Philipp Kukura, Yuliya Gordiyenko, Walid A. Houry, Larissa Höll, Sadhna Phanse, Nardin Nano, Vaibhav Bhandari, Carolina Colleti

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Structure

R2TP is a highly conserved chaperone complex formed by two AAA+ ATPases, RUVBL1 and RUVBL2, that associate with PIH1D1 and RPAP3 proteins. R2TP acts in promoting macromolecular complex formation. Here, we establish the principles of R2TP assembly. Th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48fe23d7fd00311e1248fe2b4e696e04
https://doi.org/10.1016/j.bpj.2021.11.1122