1slb: Difference between revisions

Revision as of 04:56, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1slb.png

Template:STRUCTURE 1slb

X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (GALECTIN-1) BY BIANTENNARY COMPLEX TYPE SACCHARIDESX-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (GALECTIN-1) BY BIANTENNARY COMPLEX TYPE SACCHARIDES

Template:ABSTRACT PUBMED 7773775

About this StructureAbout this Structure

1SLB is a Single protein structure. Full crystallographic information is available from OCA.

ReferenceReference

Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides., Bourne Y, Bolgiano B, Liao DI, Strecker G, Cantau P, Herzberg O, Feizi T, Cambillau C, Nat Struct Biol. 1994 Dec;1(12):863-70. PMID:7773775

Page seeded by OCA on Mon Jul 28 04:56:14 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1slb.gif|left|200px]]
+{{Seed}}
+[[Image:1slb.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1slb|  PDB=1slb  |  SCENE=  }}
-'''X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (GALECTIN-1) BY BIANTENNARY COMPLEX TYPE SACCHARIDES'''
+===X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (GALECTIN-1) BY BIANTENNARY COMPLEX TYPE SACCHARIDES===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7773775}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7773775 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7773775}}
 ==About this Structure==
@@ Line 23: / Line 27: @@
 [[Category: Bourne, Y.]]
 [[Category: Cambillau, C.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:50:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:56:14 2008''