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1zgr

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(New page: 200px<br /><applet load="1zgr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zgr, resolution 2.50&Aring;" /> '''Crystal structure of...)
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caption="1zgr, resolution 2.50&Aring;" />
'''Crystal structure of the Parkia platycephala seed lectin'''<br />
'''Crystal structure of the Parkia platycephala seed lectin'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1ZGR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Parkia_platycephala Parkia platycephala]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZGR OCA].
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1ZGR is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: Parkia platycephala]]
[[Category: Parkia platycephala]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Calvete, J.J.]]
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[[Category: Calvete, J J.]]
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[[Category: Cavada, B.S.]]
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[[Category: Cavada, B S.]]
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[[Category: Sol, F.Gallego.del.]]
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[[Category: Sol, F Gallego del.]]
[[Category: beta-prism]]
[[Category: beta-prism]]
[[Category: lectin]]
[[Category: lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:26:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:21 2008''

Revision as of 14:15, 21 February 2008


1zgr, resolution 2.50Å

Drag the structure with the mouse to rotate

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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