1JV4
Crystal structure of recombinant major mouse urinary protein (rmup) at 1.75 A resolution
Summary for 1JV4
| Entry DOI | 10.2210/pdb1jv4/pdb |
| Related | 1df3 |
| Descriptor | Major urinary protein 2, CADMIUM ION, 2-(SEC-BUTYL)THIAZOLE, ... (4 entities in total) |
| Functional Keywords | lipocalin recombinant beta barrel, transport protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Secreted: P11589 |
| Total number of polymer chains | 1 |
| Total formula weight | 19661.98 |
| Authors | Kuser, P.R.,Franzoni, L.,Ferrari, E.,Spisni, A.,Polikarpov, I. (deposition date: 2001-08-28, release date: 2001-12-05, Last modification date: 2024-10-30) |
| Primary citation | Kuser, P.R.,Franzoni, L.,Ferrari, E.,Spisni, A.,Polikarpov, I. The X-ray structure of a recombinant major urinary protein at 1.75 A resolution. A comparative study of X-ray and NMR-derived structures. Acta Crystallogr.,Sect.D, 57:1863-1869, 2001 Cited by PubMed Abstract: Major urinary proteins belong to the lipocalin family and are present in the urine of rodents as an ensemble of isoforms with pheromonal activity. The crystal structure of a recombinant mouse MUP (rMUP) was solved by the molecular-replacement technique and refined to an R factor and R(free) of 20 and 26.5%, respectively, at 1.75 A resolution. The structure was compared with an NMR model and with a crystallographic structure of the wild-type form of the protein. The crystal structures determined in different space groups present significantly smaller conformational differences amongst themselves than in comparison with NMR models. Some, but not all, of the conformational differences between the crystal and solution structures can be explained by the influence of crystallographic contacts. Most of the differences between the NMR and X-ray structures were found in the N-terminus and loop regions. A number of side chains lining the hydrophobic pocket of the molecule are more tightly packed in the NMR structure than in the crystallographic model. Surprisingly, clear and continuous electron density for a ligand was observed inside the hydrophobic pocket of this recombinant protein. Conformation of the ligand modelled inside the density is coherent with the results of recent NMR experiments. PubMed: 11717500DOI: 10.1107/S090744490101825X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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