3wg2
Crystal structure of Agrocybe cylindracea galectin mutant (N46A)Crystal structure of Agrocybe cylindracea galectin mutant (N46A)
Structural highlights
Publication Abstract from PubMedA 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
|
|