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- W2051208977 abstract "Three-dimensional electron microscopy reconstructions of the human α<sub>2</sub>-macroglobulin (α<sub>2</sub>M) dimer and chymotrypsin-transformed α<sub>2</sub>M reveal the structural arrangement of the two dimers that comprise native and proteinase-transformed molecules. They consist of two side-by-side extended strands that have a clockwise and counterclockwise twist about their major axes in the native and transformed structures, respectively. This and other studies show that there are major contacts between the two strands at both ends of the molecule that evidently sequester the receptor binding domains. Upon proteinase cleavage of the bait domains and subsequent thiol ester cleavages, which occur near the central region of the molecule, the two strands separate by 40 Å at both ends of the structure to expose the receptor binding domains and form the arm-like extensions of the transformed α<sub>2</sub>M. During the transformation of the structure, the strands untwist to expose the α<sub>2</sub>M central cavity to the proteinase. This extraordinary change in the architecture of α<sub>2</sub>M functions to completely engulf two molecules of chymotrypsin within its central cavity and to irreversibly encapsulate them." @default.
- W2051208977 created "2016-06-24" @default.
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- W2051208977 date "2002-08-01" @default.
- W2051208977 modified "2023-10-16" @default.
- W2051208977 title "The Three-dimensional Structure of the Human α2-Macroglobulin Dimer Reveals Its Structural Organization in the Tetrameric Native and Chymotrypsin α2-Macroglobulin Complexes" @default.
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- W2051208977 doi "https://doi.org/10.1074/jbc.m202714200" @default.
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