1dlp: Difference between revisions

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New page: left|200px<br /><applet load="1dlp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dlp, resolution 3.3Å" /> '''STRUCTURAL CHARACTERI...
 
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[[Image:1dlp.gif|left|200px]]<br /><applet load="1dlp" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dlp.gif|left|200px]]<br /><applet load="1dlp" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dlp, resolution 3.3&Aring;" />
caption="1dlp, resolution 3.3&Aring;" />
'''STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN'''<br />
'''STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN'''<br />


==Overview==
==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.
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==
==About this Structure==
1DLP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hyacinthoides_hispanica Hyacinthoides hispanica]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DLP OCA].  
1DLP is a [http://en.wikipedia.org/wiki/Single_protein 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==
Line 13: Line 13:
[[Category: Hyacinthoides hispanica]]
[[Category: Hyacinthoides hispanica]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Allen, A.K.]]
[[Category: Allen, A K.]]
[[Category: Donovan, M.J.]]
[[Category: Donovan, M J.]]
[[Category: Peumans, W.J.]]
[[Category: Peumans, W J.]]
[[Category: Reynolds, C.D.]]
[[Category: Reynolds, C D.]]
[[Category: Rizkallah, P.J.]]
[[Category: Rizkallah, P J.]]
[[Category: VanDamme, E.J.M.]]
[[Category: VanDamme, E J.M.]]
[[Category: Wright, L.M.]]
[[Category: Wright, L M.]]
[[Category: beta prism ii fold]]
[[Category: beta prism ii fold]]
[[Category: native]]
[[Category: native]]
[[Category: two-domain lectin]]
[[Category: two-domain lectin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:17:39 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:52 2008''

Revision as of 10:17, 21 February 2008

File:1dlp.gif


1dlp, resolution 3.3Å

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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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