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3OYW

Crystal structure of human galectin-1 in complex with thiodigalactoside

Summary for 3OYW
Entry DOI10.2210/pdb3oyw/pdb
Related3OY8
Related PRD IDPRD_900027
DescriptorGalectin-1, beta-D-galactopyranose-(1-1)-1-thio-beta-D-galactopyranose, ... (4 entities in total)
Functional Keywordscarbohydrate binding protein, galectin, lactobionic acid
Biological sourceHomo sapiens (human)
More
Total number of polymer chains2
Total formula weight30192.03
Authors
Blanchard, H.,Collins, P.M. (deposition date: 2010-09-23, release date: 2010-11-03, Last modification date: 2024-10-30)
Primary citationStannard, K.A.,Collins, P.M.,Ito, K.,Sullivan, E.M.,Scott, S.A.,Gabutero, E.,Darren Grice, I.,Low, P.,Nilsson, U.J.,Leffler, H.,Blanchard, H.,Ralph, S.J.
Galectin inhibitory disaccharides promote tumour immunity in a breast cancer model
CANCER LETT., 2010
Cited by
PubMed Abstract: High level galectin-1 expression results in cancer cell evasion of the immune response, increased tumour survival and aggressive metastases. Using a galectin-1 polyclonal antibody, high levels of galectin-1 protein were shown to be expressed by breast cancer cells established from FVB/N MMTV-c-neu mice as well as by the B16F10 melanoma cell line. In mixed lymphocyte cultures using tumour cells as antigenic stimulators, addition of recombinant galectin-1 dose-dependently inhibited lymphocyte production. Disaccharides were identified that inhibited galectin-1 function and increased growth and activation of CD8(+) CTL's killing cancer cells. X-ray crystallographic structures of human galectin-1 in complex with inhibitory disaccharides revealed their mode of binding. Combining galectin-blocking carbohydrates as adjuvants with vaccine immunotherapy in vivo to promote immune responses significantly decreased tumour progression and improved the outcomes for tumour challenged mice. This is the first report showing that suitably selected galectin-1 blocking disaccharides will act as adjuvants promoting vaccine stimulated immune responses against tumours in vivo.
PubMed: 20826047
DOI: 10.1016/j.canlet.2010.08.005
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

226707

건을2024-10-30부터공개중

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