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Phylogenetic analysis of eIF4E-family members
Authors:Email author" target="_blank">Bhavesh?JoshiEmail author  Kibwe?Lee  Dennis?L?Maeder  Rosemary?Jagus
Institution:(1) Center of Marine Biotechnology, Suite 236 Columbus Center, 701 E. Pratt Street, 21202 Baltimore, MD, USA
Abstract:

Background  

Translation initiation in eukaryotes involves the recruitment of mRNA to the ribosome which is controlled by the translation factor eIF4E. eIF4E binds to the 5'-m7Gppp cap-structure of mRNA. Three dimensional structures of eIF4Es bound to cap-analogues resemble 'cupped-hands' in which the cap-structure is sandwiched between two conserved Trp residues (Trp-56 and Trp-102 of H. sapiens eIF4E). A third conserved Trp residue (Trp-166 of H. sapiens eIF4E) recognizes the7-methyl moiety of the cap-structure. Assessment of GenBank NR and dbEST databases reveals that many organisms encode a number of proteins with homology to eIF4E. Little is understood about the relationships of these structurally related proteins to each other.
Keywords:
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