3m2m

From Proteopedia

Rat galectin-1 complex with lactose

Structural highlights

3m2m is a 8 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.95Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LEG1_RAT May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Galectin-1, a beta-galactoside binding lectin involved in immunoregulation and cancer, binds natural and many synthetic multivalent glycoconjugates with an apparent glycoside cluster effect, that is, affinity above and beyond what would be expected from the concentration of the determinant sugar. Here we have analyzed the mechanism of such cluster effects in solution at physiological concentration using a fluorescence anisotropy assay with a novel fluorescent high-affinity galectin-1 binding probe. The interaction of native dimeric and monomeric mutants of rat and human galectin-1 with mono- and divalent small molecules, fetuin, asialofetuin, and human serum glycoproteins was analyzed. Surprisingly, high-affinity binding did not depend much on the dimeric state of galectin-1 and thus is due mainly to monomeric interactions of a single carbohydrate recognition domain. The mechanism for this is unknown, but one possibility includes additional interactions that high-affinity ligands make with an extended binding site on the carbohydrate recognition domain. It follows that such weak additional interactions must be important for the biological function of galectin-1 and also for the design of galectin-1 inhibitors.

Monovalent Interactions of Galectin-1.,Salomonsson E, Larumbe A, Tejler J, Tullberg E, Rydberg H, Sundin A, Khabut A, Frejd T, Lobsanov YD, Rini JM, Nilsson UJ, Leffler H Biochemistry. 2010 Oct 13. PMID:20873803^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Salomonsson E, Larumbe A, Tejler J, Tullberg E, Rydberg H, Sundin A, Khabut A, Frejd T, Lobsanov YD, Rini JM, Nilsson UJ, Leffler H. Monovalent Interactions of Galectin-1. Biochemistry. 2010 Oct 13. PMID:20873803 doi:10.1021/bi1009584