A local α-helix drives structural evolution of streptococcal M-protein affinity for host human plasminogen

Volume: 477, Issue: 9, Pages: 1613 - 1630
Published: May 5, 2020
Abstract
Plasminogen-binding group A streptococcal M-protein (PAM) is a signature surface virulence factor of specific strains of Group A Streptococcus pyogenes (GAS) and is an important tight binding protein for human plasminogen (hPg). After activation of PAM-bound hPg to the protease, plasmin (hPm), GAS cells develop invasive surfaces that are critical for their pathogenicity. PAMs are helical dimers in solution, which are sensitive to temperature...
Paper Details
Title
A local α-helix drives structural evolution of streptococcal M-protein affinity for host human plasminogen
Published Date
May 5, 2020
Volume
477
Issue
9
Pages
1613 - 1630
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