1slt

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(New page: 200px<br /><applet load="1slt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1slt, resolution 1.9&Aring;" /> '''STRUCTURE OF S-LECTIN...)
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[[Image:1slt.jpg|left|200px]]<br /><applet load="1slt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1slt, resolution 1.9&Aring;" />
caption="1slt, resolution 1.9&Aring;" />
'''STRUCTURE OF S-LECTIN, A DEVELOPMENTALLY REGULATED VERTEBRATE BETA-GALACTOSIDE BINDING PROTEIN'''<br />
'''STRUCTURE OF S-LECTIN, A DEVELOPMENTALLY REGULATED VERTEBRATE BETA-GALACTOSIDE BINDING PROTEIN'''<br />
==Overview==
==Overview==
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The crystal structure of a 14-kDa bovine spleen S-lectin complexed with, the disaccharide N-acetyllactosamine at 1.9-A resolution reveals a, surprising structural relationship to legume lectins, despite the lack of, sequence homology. Two monomers associate to form an extended, beta-sandwich, each with the same jelly roll topology typical of legume, lectins but with dramatically trimmed loops and with different dimer, association. Each monomer binds one N-acetyllactosamine molecule in a, topologically and spatially different site than that of legume lectins., The carbohydrate-binding site provides an unprecedented paradigm for, carbohydrate binding, with a unique network of salt bridges. The, specificity for beta-galactose arises from intricate interactions that, constrain the position of the O4 atom.
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The crystal structure of a 14-kDa bovine spleen S-lectin complexed with the disaccharide N-acetyllactosamine at 1.9-A resolution reveals a surprising structural relationship to legume lectins, despite the lack of sequence homology. Two monomers associate to form an extended beta-sandwich, each with the same jelly roll topology typical of legume lectins but with dramatically trimmed loops and with different dimer association. Each monomer binds one N-acetyllactosamine molecule in a topologically and spatially different site than that of legume lectins. The carbohydrate-binding site provides an unprecedented paradigm for carbohydrate binding, with a unique network of salt bridges. The specificity for beta-galactose arises from intricate interactions that constrain the position of the O4 atom.
==About this Structure==
==About this Structure==
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1SLT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with CL and CYO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SLT OCA].
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1SLT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=CYO:'>CYO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLT OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Herzberg, O.]]
[[Category: Herzberg, O.]]
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[[Category: Liao, D.I.]]
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[[Category: Liao, D I.]]
[[Category: CL]]
[[Category: CL]]
[[Category: CYO]]
[[Category: CYO]]
[[Category: lectin]]
[[Category: lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:28:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:51 2008''

Revision as of 13:02, 21 February 2008

Image:1slt.jpg

1slt, resolution 1.9Å

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STRUCTURE OF S-LECTIN, A DEVELOPMENTALLY REGULATED VERTEBRATE BETA-GALACTOSIDE BINDING PROTEIN

Overview

The crystal structure of a 14-kDa bovine spleen S-lectin complexed with the disaccharide N-acetyllactosamine at 1.9-A resolution reveals a surprising structural relationship to legume lectins, despite the lack of sequence homology. Two monomers associate to form an extended beta-sandwich, each with the same jelly roll topology typical of legume lectins but with dramatically trimmed loops and with different dimer association. Each monomer binds one N-acetyllactosamine molecule in a topologically and spatially different site than that of legume lectins. The carbohydrate-binding site provides an unprecedented paradigm for carbohydrate binding, with a unique network of salt bridges. The specificity for beta-galactose arises from intricate interactions that constrain the position of the O4 atom.

About this Structure

1SLT is a Single protein structure of sequence from [1] with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein., Liao DI, Kapadia G, Ahmed H, Vasta GR, Herzberg O, Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1428-32. PMID:8108426

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