Collagenolytic Matrix Metalloproteinase Structure–Function Relationships: Insights From Molecular Dynamics Studies

Tatyana Karabencheva-Christova, Christo Christov, Gregg Fields

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

6 Citations (Scopus)


Several members of the zinc-dependent matrix metalloproteinase (MMP) family catalyze collagen degradation. Experimental data reveal a collaboration between different MMP domains in order to achieve efficient collagenolysis. Molecular dynamics (MD) simulations have been utilized to provide atomistic details of the collagenolytic process. The triple-helical structure of collagen exhibits local regions of flexibility, with modulation of interchain salt bridges and water bridges contributing to accessibility of individual chains by the enzyme. In turn, the hemopexin-like (HPX) domain of the MMP initially binds the triple helix and facilitates the presentation of individual strands to active site in the catalytic (CAT) domain. Extensive positive and negative correlated motions are observed between the CAT and HPX domains when collagen is bound. Ultimately, the MD simulation studies have complemented structural (NMR spectroscopy, X-ray crystallography) and kinetic analyses to provide a more detailed mechanistic view of MMP-catalyzed collagenolysis.
Original languageEnglish
Title of host publicationAdvances in Protein Chemistry and Structural Biology
EditorsTatyana Karabencheva-Christova
ISBN (Print)978-0-12-811876-4
Publication statusE-pub ahead of print - 8 May 2017


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