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2v8w
From Proteopedia
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CRYSTALLOGRAPHIC AND MASS SPECTROMETRIC CHARACTERISATION OF EIF4E WITH N7-CAP DERIVATIVES
Overview
Structural complexes of the eukaryotic translation initiation factor 4E, (eIF4E) with a series of N(7)-alkylated guanosine derivative mRNA cap, analogue structures have been characterised. Mass spectrometry was used to, determine apparent gas-phase equilibrium dissociation constants (K(d)), values of 0.15 muM, 13.6 muM, and 55.7 muM for eIF4E with 7-methyl-GTP, (m(7)GTP), GTP, and GMP, respectively. For tight and specific binding to, the eIF4E mononucleotide binding site, there seems to be a clear, requirement for guanosine derivatives to possess both the delocalised, positive charge of the N(7)-methylated guanine system and at least one, phosphate group. We show that the N(7)-benzylated monophosphates, 7-benzyl-GMP (Bn(7)GMP) and 7-(p-fluorobenzyl)-GMP (FBn(7)GMP) bind eIF4E, ... [(full description)]
About this Structure
2V8W is a [Protein complex] structure of sequences from [Homo sapiens] with MGO as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystallographic and Mass Spectrometric Characterisation of eIF4E with N(7)-alkylated Cap Derivatives., Brown CJ, McNae I, Fischer PM, Walkinshaw MD, J Mol Biol. 2007 Sep 7;372(1):7-15. Epub 2007 Jun 15. PMID:17631896
Page seeded by OCA on Tue Oct 30 17:44:04 2007
Categories: Homo sapiens | Protein complex | Brown, C.J. | Fischer, P.M. | Mcnae, I. | Walkinshaw, M.D. | MGO | 4e-bp1 | Acetylation | Cap | Eif4e | Host-virus interaction | Initiation factor | M7gtp | Phosphorylation | Protein biosynthesis | Protein synthesis inhibitor | Rna-binding | Translation regulation
