Molecular dynamics study of major urinary protein-pheromone
interactions: A structural model for ligand-induced flexibility
increase

J 2006

Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase

MACEK, Pavel; Petr NOVÁK; Hana KŘÍŽOVÁ; Lukáš ŽÍDEK; Vladimír SKLENÁŘ et. al.

Basic information

Original name

Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase

Authors

MACEK, Pavel (203 Czech Republic, guarantor); Petr NOVÁK (203 Czech Republic); Hana KŘÍŽOVÁ (203 Czech Republic); Lukáš ŽÍDEK (203 Czech Republic) and Vladimír SKLENÁŘ (203 Czech Republic)

Edition

FEBS Letters, Amsterdam, Elsevier Science B.V. 2006, 0014-5793

Other information

Language

English

Type of outcome

Article in a journal

Field of Study

10600 1.6 Biological sciences

Country of publisher

Czech Republic

Confidentiality degree

is not subject to a state or trade secret

References:

URL

Impact factor

Impact factor: 3.372

RIV identification code

RIV/00216224:14310/06:00017608

Organization unit

Faculty of Science

UT WoS

000234937400052

Keywords in English

Major urinary protein; Molecular dynamics simulation; Pheromone–protein interaction; Molecular motion; TZL; Order parameter

Abstract

In the original language

Recently, two independent 15N 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 S2 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.

Links

LC06030, research and development project

Name: Biomolekulární centrum

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre

MSM 143100005, plan (intention)

Name: Strukturně-funkční vztahy biomolekul a jejich role v metabolismu

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Structure-function Relationships and their role in the Metabolism

MSM0021622413, plan (intention)

Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment

Cite

MACEK, Pavel; Petr NOVÁK; Hana KŘÍŽOVÁ; Lukáš ŽÍDEK and Vladimír SKLENÁŘ. Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase. FEBS Letters. Amsterdam: Elsevier Science B.V., 2006, vol. 580, No 1, p. 682-684. ISSN 0014-5793.

@article{701742,
   author = {Macek, Pavel and Novák, Petr and Křížová, Hana and Žídek, Lukáš and Sklenář, Vladimír},
   article_location = {Amsterdam},
   article_number = {1},
   keywords = {Major urinary protein; Molecular dynamics simulation; Pheromone–protein interaction; Molecular motion; TZL; Order parameter},
   language = {eng},
   issn = {0014-5793},
   journal = {FEBS Letters},
   title = {Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase},
   url = {http://dx.doi.org/10.1016/j.febslet.2005.12.088},
   volume = {580},
   year = {2006}
}

TY  - JOUR
ID  - 701742
AU  - Macek, Pavel - Novák, Petr - Křížová, Hana - Žídek, Lukáš - Sklenář, Vladimír
PY  - 2006
TI  - Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase
JF  - FEBS Letters
VL  - 580
IS  - 1
SP  - 682-684
EP  - 682-684
PB  - Elsevier Science B.V.
SN  - 00145793
KW  - Major urinary protein
KW  - Molecular dynamics simulation
KW  - Pheromone–protein interaction
KW  - Molecular motion
KW  - TZL
KW  - Order parameter
UR  - http://dx.doi.org/10.1016/j.febslet.2005.12.088
N2  - Recently, two independent 15N 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 S2 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.
ER  -

MACEK, Pavel; Petr NOVÁK; Hana KŘÍŽOVÁ; Lukáš ŽÍDEK and Vladimír SKLENÁŘ. Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase. \textit{FEBS Letters}. Amsterdam: Elsevier Science B.V., 2006, vol.~580, No~1, p.~682-684. ISSN~0014-5793.

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