Dynamics of major urinary protein-pheromone interactions: Insight by NMR and MD simulations

MACEK, Pavel, Petr NOVÁK, Hana KŘÍŽOVÁ, Lukáš ŽÍDEK a Vladimír SKLENÁŘ. Dynamics of major urinary protein-pheromone interactions: Insight by NMR and MD simulations. In ISMAR 2007, Program and Abstracts. Taiwan: Taiwan Magnetic Resonance Society, 2007, s. 63-63.

Základní údaje

• Originální název: Dynamics of major urinary protein-pheromone interactions: Insight by NMR and MD simulations
• Název česky: Dynamika interakce močovinového proteinu s feromonem: Studie pomocí NMR spektroskopie a MD simulací.
• Autoři: MACEK, Pavel (203 Česká republika), Petr NOVÁK (203 Česká republika), Hana KŘÍŽOVÁ (203 Česká republika), Lukáš ŽÍDEK (203 Česká republika) a Vladimír SKLENÁŘ (203 Česká republika, garant).
• Vydání: Taiwan, ISMAR 2007, Program and Abstracts, od s. 63-63, 1 s. 2007.
• Nakladatel: Taiwan Magnetic Resonance Society

Další údaje

• Originální jazyk: angličtina
• Typ výsledku: Stať ve sborníku
• Obor: 10610 Biophysics
• Stát vydavatele: Tchaj-wan
• Utajení: není předmětem státního či obchodního tajemství
• WWW: URL
• Kód RIV: RIV/00216224:14310/07:00022902
• Organizační jednotka: Přírodovědecká fakulta
• Klíčová slova anglicky: NMR; relaxation; protein-ligand interactions; internal dynamics; N-15; MD simulations
• Štítky: internal dynamics, MD simulations, N-15, NMR, protein-ligand interactions, relaxation
• Příznaky: Mezinárodní význam

Anotace

Binding of mouse pheromones to major urinary proteins (MUPs) represents a typical example of interactions between lipocalins and their small hydrophobic ligands. Previously, based on the model-free analysis of 15N relaxation data, we observed that the backbone flexibility of MUP-I increased slightly upon pheromone binding, in contrast to the decreased flexibility expected for induced-fit interactions. To shed the light on this unusual observation, we have performed an independent study adopting different methodology. Backbone dynamics of mouse major urinary protein I (MUP-I) was studied by 15N NMR relaxation at multiple temperatures for a complex of MUP-I with its natural pheromonal ligand, 2-sec-4,5-dihydrothiazole, and for the free protein. Graphical analysis of the reduced spectral density values provided an unbiased qualitative picture of the internal motions. Quantitative parameters were obtained using a simultaneous data fitting at multiple temperatures to several models of different complexity. The relaxation data were complemented by the molecular dynamics simulations. Correlation functions and frequency-dependent order parameters were calculated from the simulated motions of the amide NH vectors. Comparison of the experimental and simulated order parameters and the information about slow conformational exchanges provided a picture of the molecular motions and offered a structural explanation for the observed difference in the dynamics of the free and bound MUP-I.

Anotace česky

Binding of mouse pheromones to major urinary proteins (MUPs) represents a typical example of interactions between lipocalins and their small hydrophobic ligands. Previously, based on the model-free analysis of 15N relaxation data, we observed that the backbone flexibility of MUP-I increased slightly upon pheromone binding, in contrast to the decreased flexibility expected for induced-fit interactions. To shed the light on this unusual observation, we have performed an independent study adopting different methodology. Backbone dynamics of mouse major urinary protein I (MUP-I) was studied by 15N NMR relaxation at multiple temperatures for a complex of MUP-I with its natural pheromonal ligand, 2-sec-4,5-dihydrothiazole, and for the free protein. Graphical analysis of the reduced spectral density values provided an unbiased qualitative picture of the internal motions. Quantitative parameters were obtained using a simultaneous data fitting at multiple temperatures to several models of different complexity. The relaxation data were complemented by the molecular dynamics simulations. Correlation functions and frequency-dependent order parameters were calculated from the simulated motions of the amide NH vectors. Comparison of the experimental and simulated order parameters and the information about slow conformational exchanges provided a picture of the molecular motions and offered a structural explanation for the observed difference in the dynamics of the free and bound MUP-I.

Návaznosti

• LC06030, projekt VaV: Název: Biomolekulární centrum

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

• MSM0021622413, záměr: Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím