1kwu: Difference between revisions

New page: left|200px<br /><applet load="1kwu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kwu, resolution 1.95Å" /> '''Rat mannose binding ...
 
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[[Image:1kwu.gif|left|200px]]<br /><applet load="1kwu" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1kwu.gif|left|200px]]<br /><applet load="1kwu" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1kwu, resolution 1.95&Aring;" />
caption="1kwu, resolution 1.95&Aring;" />
'''Rat mannose binding protein A complexed with a-Me-Man'''<br />
'''Rat mannose binding protein A complexed with a-Me-Man'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1KWU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MMA, CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KWU OCA].  
1KWU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MMA:'>MMA</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWU OCA].  


==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Clark, D.A.]]
[[Category: Clark, D A.]]
[[Category: Drickamer, K.]]
[[Category: Drickamer, K.]]
[[Category: Feinberg, H.]]
[[Category: Feinberg, H.]]
[[Category: Kolatkar, A.R.]]
[[Category: Kolatkar, A R.]]
[[Category: Ng, K.K.]]
[[Category: Ng, K K.]]
[[Category: Park-Snyder, S.]]
[[Category: Park-Snyder, S.]]
[[Category: Weis, W.I.]]
[[Category: Weis, W I.]]
[[Category: CA]]
[[Category: CA]]
[[Category: CL]]
[[Category: CL]]
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[[Category: lectin]]
[[Category: lectin]]


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