1kx0: Difference between revisions
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[[Image:1kx0.gif|left|200px]]<br /><applet load="1kx0" size=" | [[Image:1kx0.gif|left|200px]]<br /><applet load="1kx0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1kx0, resolution 2.00Å" /> | caption="1kx0, resolution 2.00Å" /> | ||
'''Rat mannose protein A (H189V I207V) complexed with man-a13-man'''<br /> | '''Rat mannose protein A (H189V I207V) complexed with man-a13-man'''<br /> | ||
==Overview== | ==Overview== | ||
Mannose-binding proteins (MBPs) are C-type animal lectins that recognize | 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== | ||
1KX0 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 CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1KX0 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=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=1KX0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Clark, D | [[Category: Clark, D A.]] | ||
[[Category: Drickamer, K.]] | [[Category: Drickamer, K.]] | ||
[[Category: Feinberg, H.]] | [[Category: Feinberg, H.]] | ||
[[Category: Kolatkar, A | [[Category: Kolatkar, A R.]] | ||
[[Category: Ng, K | [[Category: Ng, K K.]] | ||
[[Category: Park-Snyder, S.]] | [[Category: Park-Snyder, S.]] | ||
[[Category: Weis, W | [[Category: Weis, W I.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: lectin]] | [[Category: lectin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:51 2008'' | ||
Revision as of 14:38, 21 February 2008
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Rat mannose protein A (H189V I207V) complexed with man-a13-man
OverviewOverview
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 StructureAbout this Structure
1KX0 is a Single protein structure of sequence from Rattus norvegicus with and as ligands. 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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