2dv9: Difference between revisions

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{{STRUCTURE_2dv9|  PDB=2dv9  |  SCENE=  }}  
{{STRUCTURE_2dv9|  PDB=2dv9  |  SCENE=  }}  


'''Crystal structure of peanut lectin GAL-BETA-1,3-GAL complex'''
===Crystal structure of peanut lectin GAL-BETA-1,3-GAL complex===




==Overview==
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Crystal structures of peanut lectin complexed with Galbeta1-3Gal, methyl-T-antigen, Galbeta1-6GalNAc, Galalpha1-3Gal and Galalpha1-6Glc and that of a crystal grown in the presence of Galalpha1-3Galbeta1-4Gal have been determined using data collected at 100 K. The use of water bridges as a strategy for generating carbohydrate specificity was previously deduced from the complexes of the lectin with lactose (Galbeta1-4Glc) and T-antigen (Galbeta1-3GalNAc). This has been confirmed by the analysis of the complexes with Galbeta1-3Gal and methyl-T-antigen (Galbeta1-3GalNAc-alpha-OMe). A detailed analysis of lectin-sugar interactions in the complexes shows that they are more extensive when the beta-anomer is involved in the linkage. As expected, the second sugar residue is ill-defined when the linkage is 1--&gt;6. There are more than two dozen water molecules which occur in the hydration shells of all structures determined at resolutions better than 2.5 A. Most of them are involved in stabilizing the structure, particularly loops. Water molecules involved in lectin-sugar interactions are also substantially conserved. The lectin molecule is fairly rigid and does not appear to be affected by changes in temperature.
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin., Natchiar SK, Srinivas O, Mitra N, Surolia A, Jayaraman N, Vijayan M, Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1413-21. Epub 2006, Oct 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17057347 17057347]
Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin., Natchiar SK, Srinivas O, Mitra N, Surolia A, Jayaraman N, Vijayan M, Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1413-21. Epub 2006, Oct 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17057347 17057347]
Crystal structure of peanut lectin, a protein with an unusual quaternary structure., Banerjee R, Mande SC, Ganesh V, Das K, Dhanaraj V, Mahanta SK, Suguna K, Surolia A, Vijayan M, Proc Natl Acad Sci U S A. 1994 Jan 4;91(1):227-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8278370 8278370]
Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex., Banerjee R, Das K, Ravishankar R, Suguna K, Surolia A, Vijayan M, J Mol Biol. 1996 Jun 7;259(2):281-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8656429 8656429]
Structural plasticity of peanut lectin: an X-ray analysis involving variation in pH, ligand binding and crystal structure., Kundhavai Natchiar S, Arockia Jeyaprakash A, Ramya TN, Thomas CJ, Suguna K, Surolia A, Vijayan M, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):211-9. Epub 2004, Jan 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14747696 14747696]
[[Category: Arachis hypogaea]]
[[Category: Arachis hypogaea]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Legume lectin]]
[[Category: Legume lectin]]
[[Category: Open quaternary structure]]
[[Category: Open quaternary structure]]
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