1slb: Difference between revisions

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[[Image:1slb.gif|left|200px]]<br /><applet load="1slb" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1slb.gif|left|200px]]<br /><applet load="1slb" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1slb, resolution 2.3Å" />

'''X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (GALECTIN-1) BY BIANTENNARY COMPLEX TYPE SACCHARIDES'''<br />

==Overview==

Galectins are beta-galactoside-binding proteins that occur intra- and, extracellularly in many animal tissues. They have been proposed to form, networks of glycoconjugates on the cell surface, where they may modulate, various cell response pathways such as growth, activation and adhesion., The high resolution X-ray crystallographic analyses of three crystal forms, of bovine galectin-1 in complex with biantennary saccharides of, N-acetyllactosamine type reveal infinite chains of lectin dimers, cross-linked through N-acetyllactosamine units located at the end of the, oligosaccharide antenna. The oligosaccharide adopts a different low energy, conformation in each of the three crystal forms.

Galectins are beta-galactoside-binding proteins that occur intra- and extracellularly in many animal tissues. They have been proposed to form networks of glycoconjugates on the cell surface, where they may modulate various cell response pathways such as growth, activation and adhesion. The high resolution X-ray crystallographic analyses of three crystal forms of bovine galectin-1 in complex with biantennary saccharides of N-acetyllactosamine type reveal infinite chains of lectin dimers cross-linked through N-acetyllactosamine units located at the end of the oligosaccharide antenna. The oligosaccharide adopts a different low energy conformation in each of the three crystal forms.

==About this Structure==

1SLB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1SLB OCA].

1SLB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLB OCA].

==Reference==

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[[Category: complex(lectin/saccharide)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 02:~~27:29 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:39 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1slb.gif|left|200px]]<br /><applet load="1slb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1slb.gif|left|200px]]<br /><applet load="1slb" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1slb, resolution 2.3&Aring;" />
 '''X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (GALECTIN-1) BY BIANTENNARY COMPLEX TYPE SACCHARIDES'''<br />
 ==Overview==
-Galectins are beta-galactoside-binding proteins that occur intra- and, extracellularly in many animal tissues. They have been proposed to form, networks of glycoconjugates on the cell surface, where they may modulate, various cell response pathways such as growth, activation and adhesion., The high resolution X-ray crystallographic analyses of three crystal forms, of bovine galectin-1 in complex with biantennary saccharides of, N-acetyllactosamine type reveal infinite chains of lectin dimers, cross-linked through N-acetyllactosamine units located at the end of the, oligosaccharide antenna. The oligosaccharide adopts a different low energy, conformation in each of the three crystal forms.
+Galectins are beta-galactoside-binding proteins that occur intra- and extracellularly in many animal tissues. They have been proposed to form networks of glycoconjugates on the cell surface, where they may modulate various cell response pathways such as growth, activation and adhesion. The high resolution X-ray crystallographic analyses of three crystal forms of bovine galectin-1 in complex with biantennary saccharides of N-acetyllactosamine type reveal infinite chains of lectin dimers cross-linked through N-acetyllactosamine units located at the end of the oligosaccharide antenna. The oligosaccharide adopts a different low energy conformation in each of the three crystal forms.
 ==About this Structure==
-SLB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SLB OCA].
+SLB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLB OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: complex(lectin/saccharide)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:27:29 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:39 2008''