2d6m: Difference between revisions

Revision as of 18:53, 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:2d6m.png

Template:STRUCTURE 2d6m

Crystal structure of mouse galectin-9 N-terminal CRD in complex with lactoseCrystal structure of mouse galectin-9 N-terminal CRD in complex with lactose

Template:ABSTRACT PUBMED 16990264

About this StructureAbout this Structure

2D6M is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition., Nagae M, Nishi N, Murata T, Usui T, Nakamura T, Wakatsuki S, Kato R, J Biol Chem. 2006 Nov 24;281(47):35884-93. Epub 2006 Sep 21. PMID:16990264

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OCA

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-'''Crystal structure of mouse galectin-9 N-terminal CRD in complex with lactose'''
+===Crystal structure of mouse galectin-9 N-terminal CRD in complex with lactose===
-==Overview==
+<!--
-The galectins are a family of beta-galactoside-binding animal lectins with a conserved carbohydrate recognition domain (CRD). They have a high affinity for small beta-galactosides, but binding specificity for complex glycoconjugates varies considerably within the family. The ligand recognition is essential for their proper function, and the structures of several galectins have suggested their mechanism of carbohydrate binding. Galectin-9 has two tandem CRDs with a short linker, and we report the crystal structures of mouse galectin-9 N-terminal CRD (NCRD) in the absence and the presence of four ligand complexes. All structures form the same dimer, which is quite different from the canonical 2-fold symmetric dimer seen for galectin-1 and -2. The beta-galactoside recognition mechanism in the galectin-9 NCRD is highly conserved among other galectins. In the apo form structure, water molecules mimic the ligand hydrogen-bond network. The galectin-9 NCRD can bind both N-acetyllactosamine (Galbeta1-4GlcNAc) and T-antigen (Galbeta1-3GalNAc) with the proper location of Arg-64. Moreover, the structure of the N-acetyllactosamine dimer (Galbeta1-4GlcNAcbeta1-3Galbeta1-4GlcNAc) complex shows a unique binding mode of galectin-9. Finally, surface plasmon resonance assay showed that the galectin-9 NCRD forms a homophilic dimer not only in the crystal but also in solution.
+The line below this paragraph, {{ABSTRACT_PUBMED_16990264}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16990264 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16990264}}
 ==About this Structure==
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 [[Category: Carbohydrate binding protein]]
 [[Category: Galectin]]
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