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Ca2+-dependent interface formation in fibrillin-1.

Sacha A Jensen1, Adam R Corbett, Vroni Knott

  • 1Division of Molecular and Cellular Biochemistry, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.

The Journal of Biological Chemistry
|January 15, 2005
PubMed
Summary
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Calcium-binding epidermal growth factor-like (cbEGF) domains show varied calcium affinities due to interdomain contacts. This flexibility is crucial for organizing proteins like fibrillin-1 in the extracellular matrix.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • The calcium-binding epidermal growth factor-like (cbEGF) domain is a prevalent structural motif in extracellular and transmembrane proteins.
  • The molecular basis for the wide range of calcium (Ca2+) binding affinities (millimolar to nanomolar) in cbEGF domains is not well understood.

Purpose of the Study:

  • To investigate the molecular determinants of Ca2+ binding affinity variation in fibrillin-1 cbEGF domains.
  • To explore the relationship between interdomain interactions and Ca2+ affinity.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Titration with chromophoric chelators
  • Site-directed mutagenesis

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Main Results:

  • Measured Ca2+ dissociation constants (K(d)) for six fibrillin-1 cbEGF domains, revealing affinities varying by five orders of magnitude.
  • Identified direct correlation between interdomain hydrophobic contacts (TB-cbEGF) and Ca2+ affinity.
  • Demonstrated Ca2+-dependent interface formation between TB-cbEGF domains in high-affinity binders.

Conclusions:

  • Calcium affinity serves as a metric for interface formation in cbEGF domain pairs, reflecting protein flexibility.
  • The cbEGF domain plays a versatile role in modulating protein regional flexibility.
  • Findings provide insights into the organization of fibrillin-1 within extracellular microfibrils.