Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase
- Author
- RAK, Alexey1 ; PYLYPENKO, Olena2 ; DUREK, Thomas1 ; WATZKE, Anja3 ; KUSHNIR, Susanna1 ; BRUNSVELD, Lucas3 ; WALDMANN, Herbert3 4 ; GOODY, Roger S1 ; ALEXANDROV, Kirill1
[1] Department of Physical Biochemistry, Max-Planck-Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
[2] Department of Biomolecular Mechanisms, Max-Planck-Institut for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany
[3] Department of Chemical Biology, Max-Planck-Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
[4] Department of Organic Chemistry, University of Dortmund, Otto-Hahn-Strasse 6, 44227 Dortmund, Germany - Source
Science (Washington, D.C.). 2003, Vol 302, Num 5645, pp 646-650, 5 p ; ref : 27 ref
- CODEN
- SCIEAS
- ISSN
- 0036-8075
- Scientific domain
- Multidisciplinary
- Publisher
- American Association for the Advancement of Science, Washington, DC
- Publication country
- United States
- Document type
- Article
- Language
- English
- Keyword (fr)
- Complexe moléculaire Dissociation GDP Inhibiteur Structure cristalline dGTPase Protéine Rab Protéine RabDGI Enzyme Esterases Hydrolases Triphosphoric monoester hydrolases
- Keyword (en)
- Molecular complex Dissociation Guanosine diphosphate Inhibitor Crystalline structure dGTPase Enzyme Esterases Hydrolases Triphosphoric monoester hydrolases
- Keyword (es)
- Complejo molecular Disociación Guanosido difosfato Inhibidor Estructura cristalina dGTPase Enzima Esterases Hydrolases Triphosphoric monoester hydrolases
- Classification
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A03 Molecular biophysics / 002A03G Structure in molecular biology / 002A03G03 Crystalline structure
- Discipline
- Molecular biophysics
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 15248731
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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DOI
10.1126/science.1087761 
https://dx.doi.org/10.1126/science.1087761
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