1slt: Difference between revisions

New page: left|200px<br /><applet load="1slt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1slt, resolution 1.9Å" /> '''STRUCTURE OF S-LECTIN...
 
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[[Image:1slt.jpg|left|200px]]<br /><applet load="1slt" size="450" color="white" frame="true" align="right" spinBox="true"  
[[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==
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.
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==
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].  
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.]]
[[Category: Liao, D.I.]]
[[Category: Liao, D I.]]
[[Category: CL]]
[[Category: CL]]
[[Category: CYO]]
[[Category: CYO]]
[[Category: lectin]]
[[Category: lectin]]


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