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Magnesium Activates Microsecond Dynamics to Regulate Integrin-Collagen Recognition.

Ana Monica Nunes1, Conceição A S A Minetti2, David P Remeta2

  • 1Department of Chemistry & Chemical Biology, Rutgers University, 610 Taylor Road, Piscataway, NJ 08854, USA; Center for Integrative Proteomics Research, Rutgers University, 174 Frelinghuysen Road, Piscataway, NJ 08854, USA.

Structure (London, England : 1993)
|June 26, 2018
PubMed
Summary
This summary is machine-generated.

Magnesium ions (Mg2+) regulate collagen binding by integrin receptors by acting as both an anchor and a dynamic switch. This metal ion influences protein dynamics, crucial for collagen recognition and integrin activation.

Keywords:
CPMG relaxation dispersionNMR spectroscopyZZ exchangecollagen interactionsconformational selectiondynamicsinduced fitintegrin α(1) I domainmagnesium regulationmetal binding

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cellular Adhesion

Background:

  • Integrin receptors mediate cell adhesion to the extracellular matrix, including collagen.
  • Metal ions, particularly magnesium (Mg2+), play a modulatory role in integrin-collagen interactions.
  • The α1β1 integrin I domain (α1I) is a key binding site for collagen.

Purpose of the Study:

  • To elucidate the role of Mg2+ in the function of the α1β1 integrin I domain.
  • To investigate how Mg2+ binding affects the dynamics and collagen-binding activity of α1I.
  • To propose a molecular mechanism for Mg2+-mediated integrin-collagen recognition.

Main Methods:

  • Nuclear magnetic resonance (NMR)-based relaxation experiments
  • Isothermal titration calorimetry (ITC)
  • Protein adhesion assays
  • Site-directed mutagenesis

Main Results:

  • Mg2+ acts as both a structural anchor and a dynamic switch for the α1I domain.
  • Mg2+ binding enhances micro- to millisecond timescale motions in residues distal to the binding site.
  • Mutagenesis of key residues affects α1I functional activity, highlighting the importance of Mg2+-induced dynamics.
  • A multistep recognition mechanism involving conformational selection and induced fit is proposed for α1I-Mg-collagen interactions.

Conclusions:

  • Mg2+ plays a multifaceted role in integrin-collagen recognition.
  • Protein dynamics regulated by Mg2+ are essential for collagen binding and integrin activation.
  • Understanding these metal-protein interactions provides insights into how metals regulate protein function.