Thermodynamic and Mechanistic Insights into Coupled Binding and Unwinding of Collagen by Matrix Metalloproteinase 1.
Collagen unwinding
Collagenolysis
Coupled equilibria
MMP
Selected and induced fit
Journal
Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R
Informations de publication
Date de publication:
06 11 2020
06 11 2020
Historique:
received:
14
07
2020
revised:
06
10
2020
accepted:
06
10
2020
pubmed:
16
10
2020
medline:
9
3
2021
entrez:
15
10
2020
Statut:
ppublish
Résumé
Local unwinding of the collagen triple helix is a necessary step for initiating the collagen degradation cascade in extracellular matrices. A few matrix metalloproteinases (MMPs) are known to support this key process, but its energetic aspects remain unknown. Here, we captured the thermodynamics of the triple helix unwinding by monitoring interactions between a collagen peptide and MMP-1(E200A) - an active-site mutant of an archetypal vertebrate collagenase - at increasing temperatures, using isothermal titration calorimetry (ITC). Coupled binding and unwinding manifests as a curved relationship between the total enthalpy change and temperature of the reaction, producing increasingly negative heat capacity change (ΔΔC
Identifiants
pubmed: 33058879
pii: S0022-2836(20)30579-9
doi: 10.1016/j.jmb.2020.10.003
pii:
doi:
Substances chimiques
Peptides
0
Collagen
9007-34-5
Collagenases
EC 3.4.24.-
MMP1 protein, human
EC 3.4.24.7
Matrix Metalloproteinase 1
EC 3.4.24.7
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5985-5993Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.