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1986•Seminars in Thrombosis and HemostasisRequires access

A Three-Dimensional Model of a Unique Proteinase Inhibitor: α2-Macroglobulin

Steven R. Feldman, Salvatore V. Pizzo

Open publisher page 4 citations

Abstract

alpha 2-Macroglobulin inhibits many proteinases by a unique mechanism termed "trapping" depicted in Figure 3A,B. This article details a mechanism by which a large proteinase, such as plasmin, binds in a molar ratio between 1 and 2 to 1 proteinase to inhibitor. The article also discusses the placement of the bait region in relation to the thiol-esters within this model. Future investigation is required to confirm the hypothesized mechanism of plasmin binding as well as the hypothesized location of the bait region.

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What this paper is about

alpha 2-Macroglobulin inhibits many proteinases by a unique mechanism termed "trapping" depicted in Figure 3A,B. This article details a mechanism by which a large proteinase, such as plasmin, binds in a molar ratio between 1 and 2 to 1 proteinase to inhibitor. The article also discusses the placement of the bait region in relation to the thiol-esters within this model. Future investigation is required to confirm the hypothesized mechanism of plasmin binding as well as the hypothesized location of the bait region.

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Available abstract

alpha 2-Macroglobulin inhibits many proteinases by a unique mechanism termed "trapping" depicted in Figure 3A,B. This article details a mechanism by which a large proteinase, such as plasmin, binds in a molar ratio between 1 and 2 to 1 proteinase to inhibitor. The article also discusses the placement of the bait region in relation to the thiol-esters within this model. Future investigation is required to confirm the hypothesized mechanism of plasmin binding as well as the hypothesized location of the bait region.

Key concepts: Plasmin, alpha-2-Macroglobulin, Proteinase inhibitor, Macroglobulin, Mechanism (biology), Chemistry, Binding site, Thiol

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