Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1IPC

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

Summary for 1IPC
Entry DOI10.2210/pdb1ipc/pdb
Related1IPB
DescriptorEUKARYOTIC TRANSLATION INITIATION FACTOR 4E, 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE (3 entities in total)
Functional Keywordsinitiation factor, protein biosynthesis, rna binding protein
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm, P-body : P06730
Total number of polymer chains1
Total formula weight25668.46
Authors
Primary citationTomoo, 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.
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
BIOCHEM.J., 362:539-544, 2002
Cited by
PubMed Abstract: 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.
PubMed: 11879179
DOI: 10.1042/0264-6021:3620539
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon