2J9Q
A novel conformation for the TPR domain of pex5p
Summary for 2J9Q
| Entry DOI | 10.2210/pdb2j9q/pdb |
| Related | 1FCH 2C0L 2C0M |
| Descriptor | PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR, STRONTIUM ION (3 entities in total) |
| Functional Keywords | transport, zellweger syndrome, protein transport |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 2 |
| Total formula weight | 72432.62 |
| Authors | Stanley, W.A.,Wilmanns, M.,Kursula, P. (deposition date: 2006-11-15, release date: 2007-04-17, Last modification date: 2023-12-13) |
| Primary citation | Stanley, W.A.,Pursiainen, N.,Garman, E.F.,Juffer, A.,Wilmanns, M.,Kursula, P. A Previously Unobserved Conformation for the Human Pex5P Receptor Suggests Roles for Intrinsic Flexibility and Rigid Domain Motions in Ligand Binding Bmc Struct.Biol., 7:24-, 2007 Cited by PubMed Abstract: 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. PubMed: 17428317DOI: 10.1186/1472-6807-7-24 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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