1zgr
From Proteopedia
|
Crystal structure of the Parkia platycephala seed lectin
Overview
The crystal structures of the apo and mannose-bound Parkia platycephala, seed lectin represent the first structure of a Mimosoideae lectin and a, novel circular arrangement of beta-prism domains, and highlight the, adaptability of the beta-prism fold as a building block in the evolution, of plant lectins. The P.platycephala lectin is a dimer both in solution, and in the crystals. Mannose binding to each of the three homologous, carbohydrate-recognition domains of the lectin occurs through different, modes, and restrains the flexibility of surface-exposed loops and residues, involved in carbohydrate recognition. The planar array of, carbohydrate-binding sites on the rim of the toroid-shaped structure of, the P.platycephala lectin dimer immediately suggests a mechanism to, promote multivalent interactions leading to cross-linking of carbohydrate, ligands as part of the host strategy against phytopredators and pathogens., The cyclic structure of the P.platycephala lectin points to the convergent, evolution of a structural principle for the construction of lectins, involved in host defense or in attacking other organisms.
About this Structure
1ZGR is a Single protein structure of sequence from Parkia platycephala. Full crystallographic information is available from OCA.
Reference
The first crystal structure of a Mimosoideae lectin reveals a novel quaternary arrangement of a widespread domain., Gallego del Sol F, Nagano C, Cavada BS, Calvete JJ, J Mol Biol. 2005 Oct 28;353(3):574-83. Epub 2005 Sep 9. PMID:16185708
Page seeded by OCA on Wed Nov 21 07:26:29 2007
