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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

ADAM-15 disintegrin-like domain structure and function

Dong Lu1, Mike Scully, Vijay Kakkar

  • 1Thrombosis Research Institute, Manresa Road, London, SW3 6LR, UK. xlu@tri-london.ac.uk

Toxins
|November 10, 2011
PubMed

Insights

Human ADAM-15 is unique among ADAM proteins for its RGD motif, crucial for binding integrin receptors. This review explores RGD-containing domains and their role in antagonizing integrin function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • ADAM proteins are transmembrane cell-surface proteins involved in adhesion and proteolysis.
  • Human ADAM-15 uniquely possesses an Arg-Gly-Asp (RGD) motif in its disintegrin-like domain, a feature common in snake venom disintegrins.
  • This RGD motif is critical for binding integrin receptors.

Purpose of the Study:

  • To review the structural characteristics of RGD-containing disintegrin-like domains.
  • To elucidate the structural features enabling antagonism of integrin function.
  • To compare these structures to the canonical RGD template.

Main Methods:

  • Structural analysis of RGD-containing disintegrin-like domains.
  • Comparison of ADAM-15 RGD motif with other disintegrins.
  • Review of literature on integrin-disintegrin interactions.

Main Results:

  • The RGD motif in ADAM-15 acts as a specific integrin ligand binding site.
  • Structural features of RGD domains dictate their antagonistic activity against integrins.
  • ADAM-15's RGD motif shares similarities with snake venom disintegrins.

Conclusions:

  • ADAM-15's RGD motif is a key mediator of integrin interactions.
  • Understanding these structures provides insights into integrin regulation.
  • This review highlights the significance of the RGD motif in ADAM-15's biological functions.
Keywords:
ADAM proteinRGD-motifSnake venom toxindisintegrinintegrin

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