1kwu: Difference between revisions

Revision as of 11:11, 2 July 2008

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File:1kwu.png

Template:STRUCTURE 1kwu

Rat mannose binding protein A complexed with a-Me-ManRat mannose binding protein A complexed with a-Me-Man

Template:ABSTRACT PUBMED 11850428

About this StructureAbout this Structure

1KWU is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Orientation of bound ligands in mannose-binding proteins. Implications for multivalent ligand recognition., Ng KK, Kolatkar AR, Park-Snyder S, Feinberg H, Clark DA, Drickamer K, Weis WI, J Biol Chem. 2002 May 3;277(18):16088-95. Epub 2002 Feb 15. PMID:11850428

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-'''Rat mannose binding protein A complexed with a-Me-Man'''
+===Rat mannose binding protein A complexed with a-Me-Man===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11850428}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11850428}}
 ==About this Structure==
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 [[Category: Calcium-binding protein]]
 [[Category: Lectin]]
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