Structural highlights
Publication Abstract from PubMed
A fungal galectin from Agrocybe cylindracea (ACG) exhibits broad binding specificity for beta-galactose-containing glycans. We determined the crystal structures of wild-type ACG and the N46A mutant, with and without glycan ligands. From these structures and a saccharide-binding analysis of the N46A mutant, we revealed that a conformational change of a unique insertion sequence containing Asn46 provides two binding modes for ACG, and thereby confers broad binding specificity. We propose that the unique sequence provides these two distinct glycan-binding modes by an induced-fit mechanism.
Conformational change of a unique sequence in a fungal galectin from Agrocybe cylindracea controls glycan ligand-binding specificity.,Kuwabara N, Hu D, Tateno H, Makyio H, Hirabayashi J, Kato R FEBS Lett. 2013 Nov 15;587(22):3620-5. doi: 10.1016/j.febslet.2013.08.046. Epub, 2013 Sep 10. PMID:24036446[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kuwabara N, Hu D, Tateno H, Makyio H, Hirabayashi J, Kato R. Conformational change of a unique sequence in a fungal galectin from Agrocybe cylindracea controls glycan ligand-binding specificity. FEBS Lett. 2013 Nov 15;587(22):3620-5. doi: 10.1016/j.febslet.2013.08.046. Epub, 2013 Sep 10. PMID:24036446 doi:http://dx.doi.org/10.1016/j.febslet.2013.08.046
