1dlp: Difference between revisions

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[[Image:1dlp.gif|left|200px]]
{{Seed}}
[[Image:1dlp.png|left|200px]]


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{{STRUCTURE_1dlp|  PDB=1dlp  |  SCENE=  }}  
{{STRUCTURE_1dlp|  PDB=1dlp  |  SCENE=  }}  


'''STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN'''
===STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN===




==Overview==
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The three-dimensional structure of a 244-residue, multivalent, fetuin-binding lectin, SCAfet, isolated from bluebell (Scilla campanulata) bulbs, has been solved at 3.3 A resolution by molecular replacement using the coordinates of the 119-residue, mannose-binding lectin, SCAman, also from bluebell bulbs. Unlike most monocot mannose-binding lectins, such as Galanthus nivalis agglutinin from snowdrop bulbs, which fold into a single domain, SCAfet contains two domains with approximately 55% sequence identity, joined by a linker peptide. Both domains are made up of a 12-stranded beta-prism II fold, with three putative carbohydrate-binding sites, one on each subdomain. SCAfet binds to the complex saccharides of various animal glycoproteins but not to simple sugars.
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{{ABSTRACT_PUBMED_10683433}}


==About this Structure==
==About this Structure==
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[[Category: Native]]
[[Category: Native]]
[[Category: Two-domain lectin]]
[[Category: Two-domain lectin]]
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