A previously unobserved conformation for the human Pex5p receptor suggests roles for intrinsic flexibility and rigid domain motions in ligand binding |
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| Authors: | Will A Stanley Niko V Pursiainen Elspeth F Garman André H Juffer Matthias Wilmanns Petri Kursula |
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| Affiliation: | (1) EMBL-Hamburg, c/o DESY, Notkestraβe 85, 22603 Hamburg, Germany;(2) Centre for Cellular and Molecular Biology, Council of Scientific and Industrial Research, Uppal Road, Hyderabad, 500 007, India;(3) Department of Biochemistry, University of Oulu, FIN-90014 Oulu, Finland;(4) Biocenter Oulu, University of Oulu, FIN-90014 Oulu, Finland;(5) Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK |
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| Abstract: | Background The C-terminal tetratricopeptide (TPR) repeat domain of Pex5p recognises proteins carrying a peroxisomal targeting signal type 1 (PTS1) tripeptide in their C-terminus. Previously, structural data have been obtained from the TPR domain of Pex5p in both the liganded and unliganded states, indicating a conformational change taking place upon cargo protein binding. Such a conformational change would be expected to play a major role both during PTS1 protein recognition as well as in cargo release into the peroxisomal lumen. However, little information is available on the factors that may regulate such structural changes. |
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