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1zgs
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(New page: 200px<br /><applet load="1zgs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zgs, resolution 2.50Å" /> '''Parkia platycephala ...)
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Revision as of 05:19, 21 November 2007
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Parkia platycephala seed lectin in complex with 5-bromo-4-chloro-3-indolyl-a-D-mannose
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
1ZGS is a Single protein structure of sequence from Parkia platycephala with XMM as ligand. 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 07:26:32 2007
