Academic Journal

The Crystal Structure of the Carboxy-Terminal Domain of Human Translation Initiation Factor eIF5

التفاصيل البيبلوغرافية
العنوان: The Crystal Structure of the Carboxy-Terminal Domain of Human Translation Initiation Factor eIF5
المؤلفون: Bieniossek, Christoph, Schütz, Patrick, Bumann, Mario, Limacher, Andreas, Usón, Isabel, Baumann, Ulrich
بيانات النشر: Academic Press
سنة النشر: 2006
المجموعة: Digital.CSIC (Consejo Superior de Investigaciones Científicas / Spanish National Research Council)
مصطلحات موضوعية: multi-factor complex, HEAT domain, eIF5, translation initiation
الوصف: The carboxy-terminal domain (CTD) of eukaryotic initiation factor 5 (eIF5) plays a central role in the formation of the multifactor complex (MFC), an important intermediate for the 43 S preinitiation complex assembly. The IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-β, and eIF3c, thus forming together with eIF2 bound Met-tRNAi Met the MFC. In this work we present the high resolution crystal structure of eIF5-CTD. This domain of the protein is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B-ε (eIF2Bε-CTD). The most striking difference in the two structures is an additional carboxy-terminal helix in eIF5. The binding sites of eIF2-β, eIF3 and eIF1 were mapped onto the structure. eIF2-β and eIF3 bind to non-overlapping patches of negative and positive electrostatic potential, respectively. © 2006 Elsevier Ltd. All rights reserved. ; This work has been supported by the Swiss National Science Foundation and the Berner Hochschulstiftung. We gratefully acknowledge the help of Clemens Schulze-Briese at beamline X06SA, SLS, PSI Villigen, Martin Walsh at beamline BM14, ESRF, Grenoble, and Gordon Leonard at ID29, ESRF, Grenoble ; Peer Reviewed
نوع الوثيقة: article in journal/newspaper
اللغة: unknown
تدمد: 0022-2836
Relation: http://dx.doi.org/10.1016/j.jmb.2006.05.021; Journal of Molecular Biology 360(2): 457-465 (2006); http://hdl.handle.net/10261/113920
DOI: 10.1016/j.jmb.2006.05.021
الاتاحة: http://hdl.handle.net/10261/113920
https://doi.org/10.1016/j.jmb.2006.05.021
Rights: none
رقم الانضمام: edsbas.A16B028
قاعدة البيانات: BASE
الوصف
تدمد:00222836
DOI:10.1016/j.jmb.2006.05.021