Interaction of mannan binding lectin with alpha2 macroglobulin via exposed oligomannose glycans: a conserved feature of the thiol ester protein family?

@article{Arnold2006InteractionOM,
  title={Interaction of mannan binding lectin with alpha2 macroglobulin via exposed oligomannose glycans: a conserved feature of the thiol ester protein family?},
  author={James N Arnold and Russell Wallis and Antony C. Willis and David J. Harvey and Louise Royle and Raymond A. Dwek and Pauline M. Rudd and Robert B Sim},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 11},
  pages={6955-63}
}
The serum collectin mannan-binding lectin (MBL) binds to oligomannose and GlcNAc-terminating glycans present on microorganisms. Using a commercial affinity chromatography resin containing immobilized MBL we screened human and mouse serum for endogenous MBL-binding targets. We isolated the serum protease inhibitor alpha(2) macroglobulin (alpha2M), a heavily glycosylated thiol ester protein (TEP) composed of four identical 180-kDa subunits, each of which has eight N-linked glycosylation sites… CONTINUE READING
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