3a5p

Publication Abstract from PubMed

Physarum polycephalum hemagglutinin I (HA1) is a 104-residue protein that is secreted to extracellular space. The crystal structure of HA1 has a beta-sandwich fold found among lectin structures, such as legume lectins and galectins. Interestingly, the beta-sandwich of HA1 lacks a jelly roll motif and is essentially composed of two simple up-and-down beta-sheets. This up-and-down beta-sheet motif is well conserved in other legume lectin-like proteins derived from animals, plants, bacteria, and viruses. It is more noteworthy that the up-and-down beta-sheet motif includes many residues that make contact with the target carbohydrates. Our NMR data demonstrate that HA1 lacking a jelly roll motif also binds to its target glycopeptide. Taken together, these data show that the up-and-down beta-sheet motif provides a fundamental scaffold for the binding of legume lectin-like proteins to the target carbohydrates, and the structure of HA1 suggests a minimal carbohydrate recognition domain.

The Structure of Physarum polycephalum Hemagglutinin I Suggests a Minimal Carbohydrate Recognition Domain of Legume Lectin Fold.,Kouno T, Watanabe N, Sakai N, Nakamura T, Nabeshima Y, Morita M, Mizuguchi M, Aizawa T, Demura M, Imanaka T, Tanaka I, Kawano K J Mol Biol. 2010 Nov 20. PMID:21094650^[1]

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