The protease associated (PA) domain in ScpA from Streptococcus pyogenes plays a role in substrate recruitment

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Submolecular probing of the complement C5a receptor–ligand binding reveals a cooperative two-site binding mechanism

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Chimeric protein probes for C5a receptors through fusion of the anaphylatoxin C5a core region with a small-molecule antagonist

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Structure of the complement C5a receptor bound to the extra-helical antagonist NDT9513727

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The PA domain is crucial for determining optimum substrate length for soybean protease C1: Structure and kinetics correlate with molecular function

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Chemokine-cleaving Streptococcus pyogenes protease SpyCEP is necessary and sufficient for bacterial dissemination within soft tissues and the respiratory tract

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Model for Substrate Interactions in C5a Peptidase from Streptococcus pyogenes: A 1.9 Å Crystal Structure of the Active Form of ScpA

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