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Status: Bibliographieeintrag

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Verfasst von:Subramanian, Sundar Raman [VerfasserIn]   i
 Singam, Ettayapuram Ramaprasad Azhagiya [VerfasserIn]   i
 Berinski, Michael [VerfasserIn]   i
 Wade, Rebecca C. [VerfasserIn]   i
Titel:Identification of an electrostatic ruler motif for sequence-specific binding of collagenase to collagen
Verf.angabe:Sundar Raman Subramanian, Ettayapuram Ramaprasad Azhagiya Singam, Michael Berinski, Venkatesan Subramanian, and Rebecca C. Wade
E-Jahr:2016
Jahr:June 1, 2016
Umfang:10 S.
Fussnoten:Special issue: J. Andrew McCammon Festschrift ; Gesehen am 26.05.2020
Titel Quelle:Enthalten in: The journal of physical chemistry <Washington, DC> / B
Ort Quelle:Washington, DC : Soc., 1997
Jahr Quelle:2016
Band/Heft Quelle:120(2016), 33, Seite 8580-8589
ISSN Quelle:1520-5207
Abstract:Sequence-specific cleavage of collagen by mammalian collagenase plays a pivotal role in cell function. Collagenases are matrix metalloproteinases that cleave the peptide bond at a specific position on fibrillar collagen. The collagenase Hemopexin-like (HPX) domain has been proposed to be responsible for substrate recognition, but the mechanism by which collagenases identify the cleavage site on fibrillar collagen is not clearly understood. In this study, Brownian dynamics simulations coupled with atomic-detail and coarse-grained molecular dynamics simulations were performed to dock matrix metalloproteinase-1 (MMP-1) on a collagen IIIα1 triple helical peptide. We find that the HPX domain recognizes the collagen triple helix at a conserved R-X11-R motif C-terminal to the cleavage site to which the HPX domain of collagen is guided electrostatically. The binding of the HPX domain between the two arginine residues is energetically stabilized by hydrophobic contacts with collagen. From the simulations and analysis of the sequences and structural flexibility of collagen and collagenase, a mechanistic scheme by which MMP-1 can recognize and bind collagen for proteolysis is proposed.
DOI:doi:10.1021/acs.jpcb.6b02573
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1021/acs.jpcb.6b02573
 DOI: https://doi.org/10.1021/acs.jpcb.6b02573
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1698796994
Verknüpfungen:→ Zeitschrift

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