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1dlp

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dlp OCA], [http://www.ebi.ac.uk/pdbsum/1dlp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dlp RCSB]</span>
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[[Category: two-domain lectin]]
[[Category: two-domain lectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:43:56 2008''

Revision as of 16:44, 30 March 2008


PDB ID 1dlp

Drag the structure with the mouse to rotate
, resolution 3.3Å
Related: 1B2P


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1DLP is a Single protein structure of sequence from Hyacinthoides hispanica. Full crystallographic information is available from OCA.

Reference

Structural characterisation of the native fetuin-binding protein Scilla campanulata agglutinin: a novel two-domain lectin., Wright LM, Reynolds CD, Rizkallah PJ, Allen AK, Van Damme EJ, Donovan MJ, Peumans WJ, FEBS Lett. 2000 Feb 18;468(1):19-22. PMID:10683433

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