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Structure paper

TitleStructural and Functional Insights into Human Re-initiation Complexes.
Journal, issue, pagesMol. Cell, Vol. 67, Issue 3, Page 447-456.e7, Year 2017
Publish dateAug 3, 2017
AuthorsMelanie Weisser / Tanja Schäfer / Marc Leibundgut / Daniel Böhringer / Christopher Herbert Stanley Aylett / Nenad Ban
External linksPubMed:28732596 / Publisher's page
KeywordsTRANSLATION / translation re-initiation complex / translation initiation factor / RNA binding protein / small ribosomal subunit / Binding Sites / Cell Cycle Proteins / Cryoelectron Microscopy / Crystallography, X-Ray / DENR protein, human / Eukaryotic Initiation Factor-2 / Eukaryotic Initiation Factors / HEK293 Cells / Humans / MCTS1 protein, human / Molecular Docking Simulation / Multiprotein Complexes / Mutation / Nucleic Acid Conformation / Oncogene Proteins / Protein Binding / Protein Conformation / RNA, Messenger / RNA, Transfer / Ribosome Subunits, Small, Eukaryotic / Structure-Activity Relationship / Transcription Initiation Site / Transcription Initiation, Genetic / Transfection / eIF2D protein, human / eukaryotic translation initiation factor
MethodsX-ray diffraction / EM (single particle)
Resolution1.8 - 4.2 A
Structure data

Human translation re-initiation complex containing eIF2D

Human 40S-eIF2D-re-initiation complex

Human 40S-eIF2D-re-initiation complex




  • homo sapiens (human)
  • Homo sapiens (human)
  • Hepatitis C virus
  • Saccharomyces cerevisiae (baker's yeast)
  • saccharomyces cerevisiae (baker's yeast)
  • hepatitis c virus

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