TY - JOUR
T1 - Quantitative structural analysis of importin-β flexibility
T2 - Paradigm for solenoid protein structures
AU - Forwood, Jade K.
AU - Lange, Allison
AU - Zachariae, Ulrich
AU - Marfori, Mary
AU - Preast, Callie
AU - Grubmüller, Helmut
AU - Stewart, Murray
AU - Corbett, Anita H.
AU - Kobe, Bostjan
N1 - MEDLINE® is the source for the MeSH terms of this document.
PY - 2010
Y1 - 2010
N2 - The structure of solenoid proteins facilitates a higher degree of flexibility than most folded proteins. In importin-ß, a nuclear import factor built from 19 tandem HEAT repeats, flexibility plays a crucial role in allowing interactions with a range of different partners. We present a comprehensive analysis of importin-ß flexibility based on a number of different approaches. We determined the crystal structure of unliganded Saccharomyces cerevisiae importin-ß (Kap95) to allow a quantitative comparison with importin-ß bound to different partners. Complementary mutagenesis, small angle X-ray scattering and molecular dynamics studies suggest that the protein samples several conformations in solution. The analyses suggest the flexibility of the solenoid is generated by cumulative small movements along its length. Importin-ß illustrates how solenoid proteins can orchestrate protein interactions in many cellular pathways.
AB - The structure of solenoid proteins facilitates a higher degree of flexibility than most folded proteins. In importin-ß, a nuclear import factor built from 19 tandem HEAT repeats, flexibility plays a crucial role in allowing interactions with a range of different partners. We present a comprehensive analysis of importin-ß flexibility based on a number of different approaches. We determined the crystal structure of unliganded Saccharomyces cerevisiae importin-ß (Kap95) to allow a quantitative comparison with importin-ß bound to different partners. Complementary mutagenesis, small angle X-ray scattering and molecular dynamics studies suggest that the protein samples several conformations in solution. The analyses suggest the flexibility of the solenoid is generated by cumulative small movements along its length. Importin-ß illustrates how solenoid proteins can orchestrate protein interactions in many cellular pathways.
UR - http://www.scopus.com/inward/record.url?scp=77956331754&partnerID=8YFLogxK
U2 - 10.1016/j.str.2010.06.015
DO - 10.1016/j.str.2010.06.015
M3 - Article
C2 - 20826343
AN - SCOPUS:77956331754
VL - 18
SP - 1171
EP - 1183
JO - Structure
JF - Structure
SN - 0969-2126
IS - 9
ER -