4dum

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dum OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dum RCSB], [http://www.ebi.ac.uk/pdbsum/4dum PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dum OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dum RCSB], [http://www.ebi.ac.uk/pdbsum/4dum PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/IF4E_HUMAN IF4E_HUMAN]] Its translation stimulation activity is repressed by binding to the complex CYFIP1-FMR1 (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates the binding to the mRNA cap.<ref>PMID:16271312</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 19:47, 25 December 2014

Co-crystal structure of eIF4E with inhibitor

4dum, resolution 2.95Å

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