Ontology highlight
ABSTRACT:
SUBMITTER: Loh PG
PROVIDER: S-EPMC2637334 | biostudies-literature | 2009 Feb
REPOSITORIES: biostudies-literature
Loh Portia G PG Yang Hsin-Sheng HS Walsh Martin A MA Wang Qing Q Wang Xiaoxing X Cheng Zhihong Z Liu Dingxiang D Song Haiwei H
The EMBO journal 20090115 3
Pdcd4 is a tumour suppressor protein. It inhibits translation through interaction with translation initiator eIF4A, resulting in the suppression of neoplastic transformation and tumour invasion. Here, we present the crystal structures of an N-terminal-truncated Pdcd4 in free form and in complex with eIF4A. Upon binding to eIF4A, Pdcd4 undergoes a marked conformational change to form a heterotrimeric complex with eIF4A, with one Pdcd4 binding to two eIF4A molecules in two different modes. The bin ...[more]