Glycoconjugate Journal

, Volume 14, Issue 3, pp 357–363

Difference in binding-site architecture of the serum-type and liver-type mannose-binding proteins

  • Reiko T Lee
  • Yuan C Lee
Article

DOI: 10.1023/A:1018574729088

Cite this article as:
Lee, R.T. & Lee, Y.C. Glycoconj J (1997) 14: 357. doi:10.1023/A:1018574729088

Abstract

The carbohydrate-recognition domains (CRDs) of the serum-type and the liver-type mannose-binding proteins (MBPs) from rat display different binding characteristics toward mannose-rich oligosaccharides derived from N-glycosides, despite the overall similarity in their binding site architecture, oligomeric status and actual binding specificity at the monosaccharide level. We found that the liver-type MBP CRD of rat (MBP-C) bound methyl glycosides of certain mannobioses and -trioses, which are part of the mannose-rich N-glycoside, more tightly than methyl α-mannopyranoside. In contrast, the serum-type MBP CRD of rat (MBP-A) bound all the methyl glycosides of manno-oligosaccharide and methyl α-mannopyranoside with similar affinities. The mannobiose and -triose most strongly bound to MBP-C CRD were Manα(1-2)Manα-OMe and Manα (1-2)Manα(1-6)Manα-OMe, respectively. From these and other data, we postulate that the binding site of MBP-C has an extended area of interaction, probably the size of a mannotriose, while MBP-A interacts essentially with one mannose residue. Abbreviations: MBP, mannose-binding protein; CRD, carbohydrate-recognition domain; BSA, bovine serum albumin; TFA-ah, 6-(trifluoroacetyl)aminohexyl; PNP, p-nitrophenyl

Mannose-binding proteins binding specificity 

Copyright information

© Chapman and Hall 1997

Authors and Affiliations

  • Reiko T Lee
    • 1
  • Yuan C Lee
    • 1
  1. 1.Department of BiologyJohns Hopkins UniversityBaltimoreUSA

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