1zgr
From Proteopedia
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| - | [[Image:1zgr.gif|left|200px]] | + | [[Image:1zgr.gif|left|200px]] |
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| - | '''Crystal structure of the Parkia platycephala seed lectin''' | + | {{Structure |
| + | |PDB= 1zgr |SIZE=350|CAPTION= <scene name='initialview01'>1zgr</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of the Parkia platycephala seed lectin''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZGR is a [ | + | 1ZGR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Parkia_platycephala Parkia platycephala]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16185708 16185708] |
[[Category: Parkia platycephala]] | [[Category: Parkia platycephala]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lectin]] | [[Category: lectin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:35:18 2008'' |
Revision as of 13:35, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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