Structural basis for leucine-rich nuclear export signal recognition by CRM1

CRM1 (also known as XPO1 and exportin 1) mediates nuclear export of hundreds of proteins through the recognition of the leucine-rich nuclear export signal (LR-NES). Here we present the 2.9 Å structure of CRM1 bound to snurportin 1 (SNUPN). Snurportin 1 binds CRM1 in a bipartite manner by means of an...

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Veröffentlicht in:	Nature 2009-04, Vol.458 (7242), p.1136-1141
Hauptverfasser:	Dong, Xiuhua, Biswas, Anindita, Süel, Katherine E., Jackson, Laurie K., Martinez, Rita, Gu, Hongmei, Chook, Yuh Min
Format:	Artikel
Sprache:	eng
Schlagworte:	Active Transport, Cell Nucleus AFFINITY BASIC BIOLOGICAL SCIENCES Binding sites Biological and medical sciences Biological transport Crystalline structure Crystallography, X-Ray DNA-ligand interactions Epitopes Exportin 1 Protein Fatty Acids, Unsaturated - pharmacology Fundamental and applied biological sciences. Psychology GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE Humanities and Social Sciences Humans Hydrophobic and Hydrophilic Interactions INHIBITION INTERFACES Karyopherins - chemistry Karyopherins - metabolism Leucine Leucine - metabolism Leukocytes Models, Molecular Molecular biophysics multidisciplinary Nuclear Export Signals - physiology Nuclear physics Properties Protein Binding - drug effects Protein Conformation PROTEINS Receptors, Cytoplasmic and Nuclear - chemistry Receptors, Cytoplasmic and Nuclear - metabolism RESIDUES Science Science (multidisciplinary) SIGNALS snRNP Core Proteins - chemistry snRNP Core Proteins - metabolism SPECIFICITY Structure in molecular biology Structure-Activity Relationship Substrate Specificity SUBSTRATES SURFACES TRANSPORT
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