2nmn: Difference between revisions

Revision as of 23:09, 27 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:2nmn.png

Template:STRUCTURE 2nmn

Crystal structure of human galectin-3 carbohydrate-recognising domain at 2.45 angstrom resolutionCrystal structure of human galectin-3 carbohydrate-recognising domain at 2.45 angstrom resolution

Template:ABSTRACT PUBMED 17327679

About this StructureAbout this Structure

2NMN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Slow diffusion of lactose out of galectin-3 crystals monitored by X-ray crystallography: possible implications for ligand-exchange protocols., Collins PM, Hidari KI, Blanchard H, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):415-9. Epub 2007, Feb 21. PMID:17327679

Page seeded by OCA on Sun Jul 27 23:08:56 2008

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

OCA

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-'''Crystal structure of human galectin-3 carbohydrate-recognising domain at 2.45 angstrom resolution'''
+===Crystal structure of human galectin-3 carbohydrate-recognising domain at 2.45 angstrom resolution===
-==Overview==
+<!--
-Galectin-3 is a multifunctional carbohydrate-binding protein that has roles in cancer progression. In addition to carbohydrate-dependent extracellular functions, galectin-3 participates in carbohydrate-independent intracellular signalling pathways, including apoptosis, via protein-protein interactions, some of which engage the carbohydrate-binding groove. When ligands bind within this site, conformational rearrangements are induced and information on unliganded galectin-3 is therefore valuable for structure-based drug design. Removal of cocrystallized lactose from the human galectin-3 carbohydrate-recognition domain was achieved via crystal soaking, but took weeks despite low affinity. Pre-soaking to remove lactose enabled the subsequent binding of cryoprotectant glycerol, whereas when the lactose was not removed a priori the glycerol could not displace it in the short cryosoaking time frame. This slow diffusion of lactose out of the crystals contrasts with the entrance of glycerol, which takes place within minutes. The importance of the removal of incumbent ligands prior to attempts to introduce alternative ligands is indicated, even for proteins exhibiting low affinity for ligands, and has significance for ligand exchange in structure-based drug design.
+The line below this paragraph, {{ABSTRACT_PUBMED_17327679}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17327679}}
 ==About this Structure==
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 [[Category: Collins, P M.]]
 [[Category: Beta sandwich]]
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