1ipc

From Proteopedia

Revision as of 14:03, 15 February 2008

CRYSTAL STRUCTURE OF EUKARYOTIC INITIATION FACTOR 4E COMPLEXED WITH 7-METHYL GTP

Overview

The crystal structures of the full-length human eukaryotic initiation, factor (eIF) 4E complexed with two mRNA cap analogues [7-methylguanosine, 5'-triphosphate (m(7)GTP) and, P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate (m(7)GpppA)] were, determined at 2.0 A resolution (where 1 A=0.1 nm). The flexibility of the, C-terminal loop region of eIF4E complexed with m(7)GTP was significantly, reduced when complexed with m(7)GpppA, suggesting the importance of the, second nucleotide in the mRNA cap structure for the biological function of, eIF4E, especially the fixation and orientation of the C-terminal loop, region, including the eIF4E phosphorylation residue. The present results, provide the structural basis for the biological function of both N- and, C-terminal mobile regions of eIF4E in translation initiation, especially, the regulatory function through the switch-on/off of eIF4E-binding, protein-eIF4E phosphorylation.

About this Structure

1IPC is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structures of 7-methylguanosine 5'-triphosphate (m(7)GTP)- and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E: biological importance of the C-terminal flexible region., Tomoo K, Shen X, Okabe K, Nozoe Y, Fukuhara S, Morino S, Ishida T, Taniguchi T, Hasegawa H, Terashima A, Sasaki M, Katsuya Y, Kitamura K, Miyoshi H, Ishikawa M, Miura K, Biochem J. 2002 Mar 15;362(Pt 3):539-44. PMID:11879179

Page seeded by OCA on Fri Feb 15 16:03:12 2008