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Titolo:
The X-ray structure of a recombinant major urinary protein at 1.75 angstrom resolution. A comparative study of X-ray and NMR-derived structures
Autore:
Kuser, PR; Franzoni, L; Ferrari, E; Spisni, A; Polikarpov, I;
Indirizzi:
Univ Parma, Dept Expt Med, Sect Chem & Struct Biochem, I-43100 Parma, Italy Univ Parma Parma Italy I-43100 em & Struct Biochem, I-43100 Parma, Italy Lab Nacl Luz Sincrotron, BR-13084971 Campinas, SP, Brazil Lab Nacl Luz Sincrotron Campinas SP Brazil BR-13084971 BCinas, SP, Brazil
Titolo Testata:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
, volume: 57, anno: 2001,
parte:, 12
pagine: 1863 - 1869
SICI:
0907-4449(200112)57:<1863:TXSOAR>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
PUTATIVE PHEROMONE RECEPTORS; PYRAZINE-BINDING PROTEIN; BETA-LACTOGLOBULIN; FEMALE MICE; GENE FAMILY; MOUSE; CRYSTALLOGRAPHY; LIPOCALIN; DIFFRACTION; LIVER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Spisni, A Univ Parma, Dept Expt Med, Sect Chem & Struct Biochem, Via Volturno 39, I-43100 Parma, Italy Univ Parma Via Volturno 39 Parma Italy I-43100 100 Parma, Italy
Citazione:
P.R. Kuser et al., "The X-ray structure of a recombinant major urinary protein at 1.75 angstrom resolution. A comparative study of X-ray and NMR-derived structures", ACT CRYST D, 57, 2001, pp. 1863-1869

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 Angstrom 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 spacegroups 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 06:56:02