1v6k: Difference between revisions
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'''Peanut lectin-lactose complex in the presence of peptide(IWSSAGNVA)''' | {{Structure | ||
|PDB= 1v6k |SIZE=350|CAPTION= <scene name='initialview01'>1v6k</scene>, resolution 2.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Peanut lectin-lactose complex in the presence of peptide(IWSSAGNVA)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1V6K is a [ | 1V6K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V6K OCA]. | ||
==Reference== | ==Reference== | ||
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:// | 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: protein crystallography]] | [[Category: protein crystallography]] | ||
''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 14:41:27 2008'' | ||
Revision as of 15:41, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Peanut lectin-lactose complex in the presence of peptide(IWSSAGNVA)
OverviewOverview
Until recently, it has only been possible to grow crystals of peanut lectin when complexed with sugar ligands. It is now shown that it is possible to grow peanut lectin crystals at acidic pH in the presence of oligopeptides corresponding to a loop in the lectin molecule. Crystals have also been prepared in the presence of these peptides as well as lactose. Low-pH crystal forms of the lectin-lactose complex similar to those obtained at neutral pH have also been grown. Thus, crystals of peanut lectin grown under different environmental conditions, at two pH values with and without sugar bound to the lectin, are now available. They have been used to explore the plasticity and hydration of the molecule. A detailed comparison between different structures shows that the lectin molecule is sturdy and that the effect of changes in pH, ligand binding and environment on it is small. The region involving the curved front beta-sheet and the loops around the second hydrophobic core is comparatively rigid. The back beta-sheet involved in quaternary association, which exhibits considerable variability, is substantially flexible, as is the sugar-binding region. The numbers of invariant water molecules in the hydration shell are small and they are mainly involved in metal coordination or in stabilizing unusual structural features. Small consistent movements occur in the combining site upon sugar binding, although the site is essentially preformed.
About this StructureAbout this Structure
1V6K is a Single protein structure of sequence from Arachis hypogaea. Full crystallographic information is available from OCA.
ReferenceReference
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:14747696
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