1ugx: Difference between revisions

Revision as of 14:32, 28 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:1ugx.png

Template:STRUCTURE 1ugx

Crystal structure of jacalin- Me-alpha-T-antigen (Gal-beta(1-3)-GalNAc-alpha-o-Me) complexCrystal structure of jacalin- Me-alpha-T-antigen (Gal-beta(1-3)-GalNAc-alpha-o-Me) complex

Template:ABSTRACT PUBMED 12946359

About this StructureAbout this Structure

1UGX is a Protein complex structure of sequences from Artocarpus integrifolia. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of the carbohydrate specificities of jacalin: an X-ray and modeling study., Jeyaprakash AA, Katiyar S, Swaminathan CP, Sekar K, Surolia A, Vijayan M, J Mol Biol. 2003 Sep 5;332(1):217-28. PMID:12946359

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

OCA

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-[[Image:1ugx.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1ugx|  PDB=1ugx  |  SCENE=  }}
-'''Crystal structure of jacalin- Me-alpha-T-antigen (Gal-beta(1-3)-GalNAc-alpha-o-Me) complex'''
+===Crystal structure of jacalin- Me-alpha-T-antigen (Gal-beta(1-3)-GalNAc-alpha-o-Me) complex===
-==Overview==
+<!--
-The structures of the complexes of tetrameric jacalin with Gal, Me-alpha-GalNAc, Me-alpha-T-antigen, GalNAcbeta1-3Gal-alpha-O-Me and Galalpha1-6Glc (mellibiose) show that the sugar-binding site of jacalin has three components: the primary site, secondary site A, and secondary site B. In these structures and in the two structures reported earlier, Gal or GalNAc occupy the primary site with the anomeric carbon pointing towards secondary site A. The alpha-substituents, when present, interact, primarily hydrophobically, with secondary site A which has variable geometry. O-H..., centered pi and C-H...pi hydrogen bonds involving this site also exist. On the other hand, beta-substitution leads to severe steric clashes. Therefore, in complexes involving beta-linked disaccharides, the reducing sugar binds at the primary site with the non-reducing end located at secondary site B. The interactions at secondary site B are primarily through water bridges. Thus, the nature of the linkage determines the mode of the association of the sugar with jacalin. The interactions observed in the crystal structures and modeling based on them provide a satisfactory qualitative explanation of the available thermodynamic data on jacalin-carbohydrate interactions. They also lead to fresh insights into the nature of the binding of glycoproteins by jacalin.
+The line below this paragraph, {{ABSTRACT_PUBMED_12946359}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12946359 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12946359}}
 ==About this Structure==
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 [[Category: Beta-prism i fold]]
 [[Category: Galactose-specific]]
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