2bve: Difference between revisions
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==Overview== | ==Overview== | ||
The Siglec family of receptors mediates cell-surface interactions through | The Siglec family of receptors mediates cell-surface interactions through recognition of sialylated glycoconjugates. Previously reported structures of the N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various sialic acid analogs revealed the structural template for sialic acid binding. To characterize further the carbohydrate-binding properties, we have determined the crystal structures of SnD1 in the absence of ligand, and in complex with 2-benzyl-Neu5NPro and 2-benzyl-Neu5NAc. These structures reveal that SnD1 undergoes very few structural changes on ligand binding and detail how two novel classes of sialic acid analogs bind, one of which unexpectedly can induce Siglec dimerization. In conjunction with in silico analysis, this set of structures informs us about the design of putative ligands with enhanced binding affinities and specificities to different Siglecs, and provides data with which to test the effectiveness of different computational drug design protocols. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brossmer, R.]] | [[Category: Brossmer, R.]] | ||
[[Category: Burtnick, L | [[Category: Burtnick, L D.]] | ||
[[Category: Crocker, P.]] | [[Category: Crocker, P.]] | ||
[[Category: Jones, E | [[Category: Jones, E Y.]] | ||
[[Category: Kelm, S.]] | [[Category: Kelm, S.]] | ||
[[Category: May, A | [[Category: May, A P.]] | ||
[[Category: Robinson, R | [[Category: Robinson, R C.]] | ||
[[Category: Zaccai, N | [[Category: Zaccai, N R.]] | ||
[[Category: PH5]] | [[Category: PH5]] | ||
[[Category: carbohydrate binding]] | [[Category: carbohydrate binding]] | ||
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[[Category: siglec]] | [[Category: siglec]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:01 2008'' | ||
Revision as of 17:42, 21 February 2008
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STRUCTURE OF THE N-TERMINAL OF SIALOADHESIN IN COMPLEX WITH 2-PHENYL-PROP5AC
OverviewOverview
The Siglec family of receptors mediates cell-surface interactions through recognition of sialylated glycoconjugates. Previously reported structures of the N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various sialic acid analogs revealed the structural template for sialic acid binding. To characterize further the carbohydrate-binding properties, we have determined the crystal structures of SnD1 in the absence of ligand, and in complex with 2-benzyl-Neu5NPro and 2-benzyl-Neu5NAc. These structures reveal that SnD1 undergoes very few structural changes on ligand binding and detail how two novel classes of sialic acid analogs bind, one of which unexpectedly can induce Siglec dimerization. In conjunction with in silico analysis, this set of structures informs us about the design of putative ligands with enhanced binding affinities and specificities to different Siglecs, and provides data with which to test the effectiveness of different computational drug design protocols.
About this StructureAbout this Structure
2BVE is a Single protein structure of sequence from Mus musculus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic and in silico analysis of the sialoside-binding characteristics of the Siglec sialoadhesin., Zaccai NR, May AP, Robinson RC, Burtnick LD, Crocker PR, Brossmer R, Kelm S, Jones EY, J Mol Biol. 2007 Feb 2;365(5):1469-79. Epub 2006 Oct 28. PMID:17137591
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