RGD Reference Report - Orientation of bound ligands in mannose-binding proteins. Implications for multivalent ligand recognition. - Rat Genome Database

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Orientation of bound ligands in mannose-binding proteins. Implications for multivalent ligand recognition.

Authors: Ng, Kenneth K-S  Kolatkar, Anand R  Park-Snyder, Shaun  Feinberg, Hadar  Clark, Damon A  Drickamer, Kurt  Weis, William I 
Citation: Ng KK, etal., J Biol Chem. 2002 May 3;277(18):16088-95. doi: 10.1074/jbc.M200493200. Epub 2002 Feb 15.
RGD ID: 13792540
Pubmed: PMID:11850428   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M200493200   (Journal Full-text)

Mannose-binding proteins (MBPs) are C-type animal lectins that recognize high mannose oligosaccharides on pathogenic cell surfaces. MBPs bind to their carbohydrate ligands by forming a series of Ca(2+) coordination and hydrogen bonds with two hydroxyl groups equivalent to the 3- and 4-OH of mannose. In this work, the determinants of the orientation of sugars bound to rat serum and liver MBPs (MBP-A and MBP-C) have been systematically investigated. The crystal structures of MBP-A soaked with monosaccharides and disaccharides and also the structure of the MBP-A trimer cross-linked by a high mannose asparaginyl oligosaccharide reveal that monosaccharides or alpha1-6-linked mannose bind to MBP-A in one orientation, whereas alpha1-2- or alpha1-3-linked mannose binds in an orientation rotated 180 degrees around a local symmetry axis relating the 3- and 4-OH groups. In contrast, a similar set of ligands all bind to MBP-C in a single orientation. The mutation of MBP-A His(189) to its MBP-C equivalent, valine, causes Man alpha 1-3Man to bind in a mixture of orientations. These data combined with modeling indicate that the residue at this position influences the orientation of bound ligands in MBP. We propose that the control of binding orientation can influence the recognition of multivalent ligands. A lateral association of trimers in the cross-linked crystals may reflect interactions within higher oligomers of MBP-A that are stabilized by multivalent ligands.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Mbl1Ratprotein homotrimerization involved_inIDA PMID:11850428UniProt 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Mbl1Ratcalcium ion binding enablesIDA PMID:11850428UniProt 
Mbl1Ratcalcium-dependent carbohydrate binding enablesIDA PMID:11850428UniProt 
Mbl1RatD-mannose binding enablesIDA PMID:11850428UniProt 
Mbl1Ratoligosaccharide binding enablesIDA PMID:11850428UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Mbl1  (mannose binding lectin 1)


Additional Information