1dlp: Difference between revisions
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[[Image:1dlp.gif|left|200px]] | [[Image:1dlp.gif|left|200px]] | ||
'''STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN''' | {{Structure | ||
|PDB= 1dlp |SIZE=350|CAPTION= <scene name='initialview01'>1dlp</scene>, resolution 3.3Å | |||
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|LIGAND= | |||
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'''STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DLP is a [ | 1DLP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hyacinthoides_hispanica Hyacinthoides hispanica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLP OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10683433 10683433] | ||
[[Category: Hyacinthoides hispanica]] | [[Category: Hyacinthoides hispanica]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: two-domain lectin]] | [[Category: two-domain lectin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:40:27 2008'' | ||
Revision as of 08:40, 20 March 2008
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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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