2nmo

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[[Image:2nmo.jpg|left|200px]]
[[Image:2nmo.jpg|left|200px]]
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{{Structure
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|PDB= 2nmo |SIZE=350|CAPTION= <scene name='initialview01'>2nmo</scene>, resolution 1.35&Aring;
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The line below this paragraph, containing "STRUCTURE_2nmo", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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{{STRUCTURE_2nmo| PDB=2nmo | SCENE= }}
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|RELATEDENTRY=[[2nmn|2NMN]], [[2nn8|2NN8]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nmo OCA], [http://www.ebi.ac.uk/pdbsum/2nmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nmo RCSB]</span>
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'''Crystal structure of human galectin-3 carbohydrate-recognition domain at 1.35 angstrom resolution'''
'''Crystal structure of human galectin-3 carbohydrate-recognition domain at 1.35 angstrom resolution'''
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[[Category: Blanchard, H.]]
[[Category: Blanchard, H.]]
[[Category: Collins, P M.]]
[[Category: Collins, P M.]]
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[[Category: beta-sandwich]]
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[[Category: Beta-sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:38:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:05:14 2008''
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Revision as of 06:38, 4 May 2008

Template:STRUCTURE 2nmo

Crystal structure of human galectin-3 carbohydrate-recognition domain at 1.35 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.

About this Structure

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

Reference

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 May 4 09:38:16 2008

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