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The second type II module from human matrix metalloproteinase 2: structure, function and dynamics.

K Briknarová1, A Grishaev, L Bányai

  • 1Department of Chemistry Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, PA 15213, USA.

Structure (London, England : 1993)
|November 5, 1999
PubMed
Summary

Matrix metalloproteinase 2 (MMP-2) binds collagen via its second type II module (col-2). This interaction involves specific aromatic residues and a Glycine-rich segment, crucial for extracellular matrix remodeling.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Matrix metalloproteinase 2 (MMP-2) is vital for extracellular matrix degradation, influencing cell migration, tissue remodeling, and various pathological processes.
  • MMP-2 cleaves collagen, elastin, fibronectin, and laminin, with collagen binding facilitated by fibronectin type II homologous repeats within its catalytic domain.

Purpose of the Study:

  • To determine the NMR solution structure of the second type II module (col-2) of human MMP-2.
  • To investigate the interaction between the col-2 module and collagen.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used to determine the solution structure of the col-2 module.
  • (15)N relaxation experiments were performed to analyze backbone amide dynamics.

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  • Interaction studies were conducted using a synthetic peptide mimicking the collagen consensus sequence, (Pro-Pro-Gly)(6).

    • Main Results:

    • The NMR structure revealed a typical type II fold for col-2, characterized by beta sheets and loops surrounding conserved aromatic residues.
    • Backbone amide dynamics correlated with solvent accessibility and hydrogen bonding patterns.
    • The col-2 module demonstrated interaction with the synthetic collagen peptide (Pro-Pro-Gly)(6).

    Conclusions:

    • The binding surface of col-2 for collagen involves exposed aromatic residues (Phe21, Tyr38, Trp40, Tyr47, Tyr53, Phe55) and the Gly33-Gly37 segment.
    • These findings elucidate the molecular basis of MMP-2's collagen-binding activity.
    • Understanding this interaction is key to comprehending MMP-2's role in physiological and pathological processes.