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α-Macroglobulin inhibits a broad spectrum of
proteinases by forming macromolecular cages inside which
proteinases are cross-linked and trapped. Upon formation
of a complex with proteinase, α-macroglobulin undergoes
a large conformational change that results in the exposure
of its receptor-binding domain (RBD). Engagement of this
domain by α-macroglobulin receptor permits clearance
of the α-macroglobulin: proteinase complex from circulation.
The crystal structure of rat α1-macroglobulin
RBD has been determined at 2.3 Å resolution. The
RBD is composed of a nine-stranded β-sandwich and a
single α-helix that has been implicated as part of
the receptor binding site and that lies on the surface
of the β-sandwich. The crystallographic asymmetric
unit contains a dimer of RBDs related by approximate twofold
symmetry such that the putative receptor recognition sites
of the two monomers are contiguous. By gel filtration and
ultracentrifugation, it is shown that RBD dimers form in
solution with a dissociation constant of ∼50 μM.
The structure of the RBD dimer might mimic a conformation
of transformed α-macroglobulin in which the proposed
receptor binding residues are exposed on one face of the
dimer. A pair of phenylalanine residues replaces a cystine
that is conserved in other members of the macroglobulin
family. These residues participate in a network of aromatic
side-chain interactions that appears to stabilize the dimer
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