1v6l

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[[Image:1v6l.png|left|200px]]
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==About this Structure==
==About this Structure==
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1V6L is a 4 chains structure with sequences 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=1V6L OCA].
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[[1v6l]] is a 4 chain structure with 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=1V6L OCA].
==Reference==
==Reference==
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[[Category: Protein crystallography]]
[[Category: Protein crystallography]]
[[Category: Sugar binding protein]]
[[Category: Sugar binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 22 14:58:46 2010''
 

Revision as of 19:23, 14 March 2011

Template:STRUCTURE 1v6l

Peanut lectin-lactose complex in the presence of 9mer peptide (PVIWSSATG)

Template:ABSTRACT PUBMED 14747696

About this Structure

1v6l is a 4 chain structure with sequence from Arachis hypogaea. Full crystallographic information is available from OCA.

Reference

  • Kundhavai Natchiar S, Arockia Jeyaprakash A, Ramya TN, Thomas CJ, Suguna K, Surolia A, Vijayan M. Structural plasticity of peanut lectin: an X-ray analysis involving variation in pH, ligand binding and crystal structure. Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):211-9. Epub 2004, Jan 23. PMID:14747696 doi:http://dx.doi.org/10.1107/S090744490302849X
  • Banerjee R, Das K, Ravishankar R, Suguna K, Surolia A, Vijayan M. Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex. J Mol Biol. 1996 Jun 7;259(2):281-96. PMID:8656429 doi:10.1006/jmbi.1996.0319
  • Ravishankar R, Thomas CJ, Suguna K, Surolia A, Vijayan M. 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. Proteins. 2001 May 15;43(3):260-70. PMID:11288176

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