1ulm
From Proteopedia
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| - | + | {{STRUCTURE_1ulm| PDB=1ulm | SCENE= }} | |
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'''Crystal Structure of Pokeweed Lectin-D2 complexed with tri-N-acetylchitotriose''' | '''Crystal Structure of Pokeweed Lectin-D2 complexed with tri-N-acetylchitotriose''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULM OCA]. | |
==Reference== | ==Reference== | ||
Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed., Hayashida M, Fujii T, Hamasu M, Ishiguro M, Hata Y, J Mol Biol. 2003 Nov 28;334(3):551-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14623194 14623194] | Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed., Hayashida M, Fujii T, Hamasu M, Ishiguro M, Hata Y, J Mol Biol. 2003 Nov 28;334(3):551-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14623194 14623194] | ||
| - | [[Category: Phytolacca americana]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Fujii, T.]] | [[Category: Fujii, T.]] | ||
[[Category: Hata, Y.]] | [[Category: Hata, Y.]] | ||
[[Category: Hayashida, M.]] | [[Category: Hayashida, M.]] | ||
[[Category: Ishiguro, M.]] | [[Category: Ishiguro, M.]] | ||
| - | [[Category: | + | [[Category: Chitin-binding]] |
| - | [[Category: | + | [[Category: Hevein domain]] |
| - | [[Category: | + | [[Category: Lectin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:23:42 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:23, 3 May 2008
Crystal Structure of Pokeweed Lectin-D2 complexed with tri-N-acetylchitotriose
Overview
The roots of pokeweed (Phytolacca americana) are known to contain the lectins designated PL-A, PL-B, PL-C, PL-D1, and PL-D2. Of these lectins, the crystal structures of two PLs, the ligand-free PL-C and the complex of PL-D2 with tri-N-acetylchitotriose, have been determined at 1.8A resolution. The polypeptide chains of PL-C and PL-D2 form three and two repetitive chitin-binding domains, respectively. In the crystal structure of the PL-D2 complex, one trisaccharide molecule is shared mainly between two neighboring molecules related to each other by a crystallographic 2(1)-screw axis, and infinite helical chains of complexed molecules are generated by the sharing of ligand molecules. The crystal structure of PL-C reveals that the molecule is a dimer of two identical subunits, whose polypeptide chains are located in a head-to-tail fashion by a molecular 2-fold axis. Three putative carbohydrate-binding sites in each subunit are located in the dimer interface. The dimerization of PL-C is performed through the hydrophobic interactions between the carbohydrate-binding sites of the opposite domains in the dimer, leading to a distinct dimerization mode from that of wheat-germ agglutinin. Three aromatic residues in each carbohydrate-binding site of PL-C are involved in the dimerization. These residues correspond to the residues that interact mainly with the trisaccharide in the PL-D2 complex and appear to mimic the saccharide residues in the complex. Consequently, the present structure of the PL-C dimer has no room for accommodating carbohydrate. The quaternary structure of PL-C formed through these putative carbohydrate-binding residues may lead to the lack of hemagglutinating activity.
About this Structure
Full crystallographic information is available from OCA.
Reference
Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed., Hayashida M, Fujii T, Hamasu M, Ishiguro M, Hata Y, J Mol Biol. 2003 Nov 28;334(3):551-65. PMID:14623194 Page seeded by OCA on Sat May 3 11:23:42 2008
