Model of alpha 2-macroglobulin structure and function.

Published

Journal Article

A model of alpha 2-macroglobulin is presented that is compatible with previous structural, functional, and phylogenetic studies of the protein. The model of the molecule resembles a hollow cylinder and is comprised of two identical functional halves with three C2 axes of symmetry and no mirror planes. The "trap mechanism" of this proteinase inhibitor is effected by slight movement of two trap arms per "half-molecule." Evidence for this model is obtained from the study of the structure and proteinase binding of the molecule. By using this model, predictions are made concerning proteinase binding ratios, receptor recognition, and "slow-to-fast" conformational change of the molecule.

Full Text

Duke Authors

Cited Authors

  • Feldman, SR; Gonias, SL; Pizzo, SV

Published Date

  • September 1985

Published In

Volume / Issue

  • 82 / 17

Start / End Page

  • 5700 - 5704

PubMed ID

  • 2412223

Pubmed Central ID

  • 2412223

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.82.17.5700

Language

  • eng

Conference Location

  • United States