Molecular dynamics study of major urinary protein-pheromone interactions: a structural model for ligand-induced flexibility increase
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
16412435
DOI
10.1016/j.febslet.2005.12.088
PII: S0014-5793(05)01573-5
Knihovny.cz E-zdroje
- MeSH
- feromony chemie metabolismus MeSH
- molekulární modely * MeSH
- počítačová simulace MeSH
- protein - isoformy chemie metabolismus MeSH
- proteiny * chemie metabolismus MeSH
- terciární struktura proteinů * MeSH
- vodíková vazba MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- feromony MeSH
- major urinary proteins MeSH Prohlížeč
- protein - isoformy MeSH
- proteiny * MeSH
Recently, two independent (15)N NMR relaxation studies indicated that in contrast to the decreased flexibility expected for induced-fit interactions, the backbone flexibility of major urinary protein isoform I (MUP-I) slightly increased upon complex formation with its natural pheromone 2-sec-butyl-4,5-dihydrothiazol. We have investigated the subtle details of molecular interactions by molecular dynamics simulations in explicit solvent. The calculated order parameters S(2) for a free- and ligand-bound protein supply evidence that mobility in various regions of MUP-I can be directly related to small conformational changes of the free- and complexed protein resulting from modifications of the hydrogen bonding network.
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