1jv4
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Crystal structure of recombinant major mouse urinary protein (rmup) at 1.75 A resolution
OverviewOverview
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.
About this StructureAbout this Structure
1JV4 is a Single protein structure of sequence from Mus musculus with CD and TZL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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., Kuser PR, Franzoni L, Ferrari E, Spisni A, Polikarpov I, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1863-9. Epub 2001, Nov 21. PMID:11717500
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