Structural highlights
1ul9 is a 2 chain structure with sequence from Copci. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Related: | 1sla, 1qmj, 1gan, 1c1f, 1bkz, 1a3k, 1lcl, 1is5, 1ulc, 1uld, 1ule, 1ulf, 1ulg |
| Gene: | cgl2 (COPCI) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[CGL2_COPCI] Binds lactose. May play a role in fruiting body formation.[1]
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
Recognition of and discrimination between potential glyco-substrates is central to the function of galectins. Here we dissect the fundamental parameters responsible for such selectivity by the fungal representative, CGL2. The 2.1 A crystal structure of CGL2 and five substrate complexes reveal that this prototype galectin achieves increased substrate specificity by accommodating substituted oligosaccharides of the mammalian blood group A/B type in an extended binding cleft. Kinetic studies on wild-type and mutant CGL2 proteins demonstrate that the tetrameric organization is essential for functionality. The geometric constraints due to the orthogonal orientation of the four binding sites have important consequences on substrate binding and selectivity.
Structure and functional analysis of the fungal galectin CGL2.,Walser PJ, Haebel PW, Kunzler M, Sargent D, Kues U, Aebi M, Ban N Structure. 2004 Apr;12(4):689-702. PMID:15062091[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cooper DN, Boulianne RP, Charlton S, Farrell EM, Sucher A, Lu BC. Fungal galectins, sequence and specificity of two isolectins from Coprinus cinereus. J Biol Chem. 1997 Jan 17;272(3):1514-21. PMID:8999822
- ↑ Walser PJ, Haebel PW, Kunzler M, Sargent D, Kues U, Aebi M, Ban N. Structure and functional analysis of the fungal galectin CGL2. Structure. 2004 Apr;12(4):689-702. PMID:15062091 doi:10.1016/j.str.2004.03.002
