1v6o: Difference between revisions

Revision as of 16:25, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1v6o.png

Template:STRUCTURE 1v6o

Peanut lectin complexed with 10mer peptide (PVRIWSSATG)Peanut lectin complexed with 10mer peptide (PVRIWSSATG)

Template:ABSTRACT PUBMED 14747696

About this StructureAbout this Structure

1V6O 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

Crystal structures of the peanut lectin-lactose complex at acidic pH: retention of unusual quaternary structure, empty and carbohydrate bound combining sites, molecular mimicry and crystal packing directed by interactions at the combining site., Ravishankar R, Thomas CJ, Suguna K, Surolia A, Vijayan M, Proteins. 2001 May 15;43(3):260-70. PMID:11288176

Page seeded by OCA on Tue Jul 29 16:24:57 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1v6o|  PDB=1v6o  |  SCENE=  }}
-'''Peanut lectin complexed with 10mer peptide (PVRIWSSATG)'''
+===Peanut lectin complexed with 10mer peptide (PVRIWSSATG)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14747696}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14747696 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14747696}}
 ==About this Structure==
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 ==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://www.ncbi.nlm.nih.gov/pubmed/14747696 14747696]
+Crystal structures of the peanut lectin-lactose complex at acidic pH: retention of unusual quaternary structure, empty and carbohydrate bound combining sites, molecular mimicry and crystal packing directed by interactions at the combining site., Ravishankar R, Thomas CJ, Suguna K, Surolia A, Vijayan M, Proteins. 2001 May 15;43(3):260-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11288176 11288176]
 [[Category: Arachis hypogaea]]
 [[Category: Single protein]]
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 [[Category: Monoclinic and peptide]]
 [[Category: Open quaternary association]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:09:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:24:57 2008''