Ontology highlight
ABSTRACT:
SUBMITTER: Martin-Benito J
PROVIDER: S-EPMC536017 | biostudies-literature | 2004 Dec
REPOSITORIES: biostudies-literature
Martín-Benito Jaime J Bertrand Sara S Hu Ting T Ludtke Paul J PJ McLaughlin Joseph N JN Willardson Barry M BM Carrascosa José L JL Valpuesta José M JM
Proceedings of the National Academy of Sciences of the United States of America 20041206 50
The three-dimensional structure of the complex formed between the cytosolic chaperonin CCT (chaperonin containing TCP-1) and phosducin (Pdc)-like protein (PhLP), a regulator of CCT activity, has been solved by cryoelectron microscopy. Binding of PhLP to CCT occurs through only one of the chaperonin rings, and the protein does not occupy the central folding cavity but rather sits above it through interactions with two regions on opposite sides of the ring. This causes the apical domains of the CC ...[more]