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1dlp

From Proteopedia

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[[Image:1dlp.png|left|200px]]
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==STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN==
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<StructureSection load='1dlp' size='340' side='right' caption='[[1dlp]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dlp]] is a 6 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DLP FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b2p|1b2p]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1dlp RCSB], [http://www.ebi.ac.uk/pdbsum/1dlp PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/1dlp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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{{STRUCTURE_1dlp| PDB=1dlp | SCENE= }}
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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<ref>PMID:10683433</ref>
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===STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_10683433}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1dlp]] is a 6 chain structure with 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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:010683433</ref><ref group="xtra">PMID:017009862</ref><references group="xtra"/>
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[[Category: Hyacinthoides hispanica]]
[[Category: Hyacinthoides hispanica]]
[[Category: Allen, A K.]]
[[Category: Allen, A K.]]

Revision as of 06:41, 4 September 2014

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

1dlp, resolution 3.30Å

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