2d3s: Difference between revisions

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{{STRUCTURE_2d3s|  PDB=2d3s  |  SCENE=  }}  
{{STRUCTURE_2d3s|  PDB=2d3s  |  SCENE=  }}  


'''Crystal Structure of basic winged bean lectin with Tn-antigen'''
===Crystal Structure of basic winged bean lectin with Tn-antigen===




==Overview==
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The crystal structure of winged bean basic agglutinin in complex with GalNAc-alpha-O-Ser (Tn-antigen) has been elucidated at 2.35 angstroms resolution in order to characterize the mode of binding of Tn-antigen with the lectin. The Gal moiety occupies the primary binding site and makes interactions similar to those found in other Gal/GalNAc specific legume lectins. The nitrogen and oxygen atoms of the acetamido group of the sugar make two hydrogen bonds with the protein atoms whereas its methyl group is stabilized by hydrophobic interactions. A water bridge formed between the terminal oxygen atoms of the serine residue of the Tn-antigen and the side chain oxygen atom of Asn128 of the lectin increase the affinity of the lectin for Tn-antigen compared to that for GalNAc. A comparison with the available structures reveals that while the interactions of the glyconic part of the antigen are conserved, the mode of stabilization of the serine residue differs and depends on the nature of the protein residues in its vicinity. The structure provides a qualitative explanation for the thermodynamic parameters of the complexation of the lectin with Tn-antigen. Modeling studies indicate the possibility of an additional hydrogen bond with the lectin when the antigen is part of a glycoprotein.
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural basis for the specificity of basic winged bean lectin for the Tn-antigen: a crystallographic, thermodynamic and modelling study., Kulkarni KA, Sinha S, Katiyar S, Surolia A, Vijayan M, Suguna K, FEBS Lett. 2005 Dec 19;579(30):6775-80. Epub 2005 Nov 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16310781 16310781]
Structural basis for the specificity of basic winged bean lectin for the Tn-antigen: a crystallographic, thermodynamic and modelling study., Kulkarni KA, Sinha S, Katiyar S, Surolia A, Vijayan M, Suguna K, FEBS Lett. 2005 Dec 19;579(30):6775-80. Epub 2005 Nov 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16310781 16310781]
Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution., Prabu MM, Sankaranarayanan R, Puri KD, Sharma V, Surolia A, Vijayan M, Suguna K, J Mol Biol. 1998 Mar 6;276(4):787-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9500920 9500920]
Structure of basic winged-bean lectin and a comparison with its saccharide-bound form., Manoj N, Srinivas VR, Suguna K, Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):794-800. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10089310 10089310]
Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin., Manoj N, Srinivas VR, Surolia A, Vijayan M, Suguna K, J Mol Biol. 2000 Oct 6;302(5):1129-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11183779 11183779]
[[Category: Psophocarpus tetragonolobus]]
[[Category: Psophocarpus tetragonolobus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Legume lectin]]
[[Category: Legume lectin]]
[[Category: Tn-antigen]]
[[Category: Tn-antigen]]
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