Next Article in Journal
Assessment of Amino Acid/Drug Transporters for Renal Transport of [18F]Fluciclovine (anti-[18F]FACBC) in Vitro
Next Article in Special Issue
Predicting Protein–Protein Interaction Sites Using Sequence Descriptors and Site Propensity of Neighboring Amino Acids
Previous Article in Journal
Effect of Genetic Polymorphisms and Long-Term Tobacco Exposure on the Risk of Breast Cancer
Previous Article in Special Issue
In Vivo Analysis of Protein–Protein Interactions with Bioluminescence Resonance Energy Transfer (BRET): Progress and Prospects
Article Menu
Issue 10 (October) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2016, 17(10), 1727; doi:10.3390/ijms17101727

Effects of Mutations on Structure–Function Relationships of Matrix Metalloproteinase-1

1
Department of Applied Sciences, Faculty of Health and Life Sciences, Northumbria University, Newcastle upon Tyne, NE1 8ST, UK
2
Department of Chemistry & Biochemistry, Florida Atlantic University, Jupiter, FL 33458, USA
3
Department of Chemistry, The Scripps Research Institute/Scripps Florida, Jupiter, FL 33458, USA
*
Authors to whom correspondence should be addressed.
Academic Editor: Charles J. Malemud
Received: 22 August 2016 / Revised: 16 September 2016 / Accepted: 3 October 2016 / Published: 14 October 2016
(This article belongs to the Collection Proteins and Protein-Ligand Interactions)
View Full-Text   |   Download PDF [7950 KB, uploaded 14 October 2016]   |  

Abstract

Matrix metalloproteinase-1 (MMP-1) is one of the most widely studied enzymes involved in collagen degradation. Mutations of specific residues in the MMP-1 hemopexin-like (HPX) domain have been shown to modulate activity of the MMP-1 catalytic (CAT) domain. In order to reveal the structural and conformational effects of such mutations, a molecular dynamics (MD) study was performed of in silico mutated residues in the X-ray crystallographic structure of MMP-1 complexed with a collagen-model triple-helical peptide (THP). The results indicate an important role of the mutated residues in MMP-1 interactions with the THP and communication between the CAT and the HPX domains. Each mutation has a distinct impact on the correlated motions in the MMP-1•THP. An increased collagenase activity corresponded to the appearance of a unique anti-correlated motion and decreased correlated motions, while decreased collagenase activity corresponded both to increased and decreased anti-correlated motions. View Full-Text
Keywords: matrix metalloproteinase-1; conformational flexibility; molecular dynamics simulations; mutations; correlated motions matrix metalloproteinase-1; conformational flexibility; molecular dynamics simulations; mutations; correlated motions
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Singh, W.; Fields, G.B.; Christov, C.Z.; Karabencheva-Christova, T.G. Effects of Mutations on Structure–Function Relationships of Matrix Metalloproteinase-1. Int. J. Mol. Sci. 2016, 17, 1727.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top