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[[Image:1ciw.gif|left|200px]]


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==PEANUT LECTIN COMPLEXED WITH N-ACETYLLACTOSAMINE==
The line below this paragraph, containing "STRUCTURE_1ciw", creates the "Structure Box" on the page.
<StructureSection load='1ciw' size='340' side='right'caption='[[1ciw]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ciw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CIW FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=PRD_900019:N-acetyl-alpha-lactosamine'>PRD_900019</scene></td></tr>
{{STRUCTURE_1ciw| PDB=1ciw |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ciw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ciw OCA], [https://pdbe.org/1ciw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ciw RCSB], [https://www.ebi.ac.uk/pdbsum/1ciw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ciw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LECG_ARAHY LECG_ARAHY] D-galactose specific lectin.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ci/1ciw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=1ciw ConSurf].
<div style="clear:both"></div>


'''PEANUT LECTIN COMPLEXED WITH N-ACETYLLACTOSAMINE'''
==See Also==
 
*[[Agglutinin 3D structures|Agglutinin 3D structures]]
 
*[[Galactose-binding lectin|Galactose-binding lectin]]
==Overview==
__TOC__
The crystal structures of complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine have been determined at 2.8 and 2.7 A, respectively. These, and the complexes involving lactose and the T-antigenic disaccharide reported previously, permit a detailed characterization of peanut-lectin-carbohydrate association and the role of water molecules therein. The water molecules in the combining site are substantially conserved in the four complexes. The role of interacting sugar hydroxyl groups, when absent, are often mimicked by ordered water molecules not only at the primary combining site, but also at the site of the second sugar ring. The similarity of peanut-lectin-sugar interactions with those in other galactose/N-acetylgalactosamine-specific lectins also extend to a substantial degree to water bridges. The comparative study provides a structural explanation for the exclusive specificity of peanut lectin for galactose at the monosaccharide level, compared with that of the other lectins for galactose as well as N-acetylgalactosamine. The complexes also provide a qualitative structural rationale for differences in the strengths of binding of peanut lectin to different sugars.
</StructureSection>
 
==About this Structure==
1CIW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIW OCA].
 
==Reference==
Structures of the complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins., Ravishankar R, Suguna K, Surolia A, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1999 Aug;55(Pt 8):1375-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10417405 10417405]
[[Category: Arachis hypogaea]]
[[Category: Arachis hypogaea]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ravishankar, R.]]
[[Category: Ravishankar R]]
[[Category: Suguna, K.]]
[[Category: Suguna K]]
[[Category: Surolia, A.]]
[[Category: Surolia A]]
[[Category: Vijayan, M.]]
[[Category: Vijayan M]]
[[Category: Agglutinin]]
[[Category: Carbohydrate specificity]]
[[Category: Lectin]]
[[Category: Legume lectin]]
[[Category: N- acetyllactosamine]]
[[Category: Protein crystallography]]
[[Category: Water bridge]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:46:48 2008''

Latest revision as of 08:57, 3 April 2024

PEANUT LECTIN COMPLEXED WITH N-ACETYLLACTOSAMINEPEANUT LECTIN COMPLEXED WITH N-ACETYLLACTOSAMINE

Structural highlights

1ciw is a 4 chain structure with sequence from Arachis hypogaea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LECG_ARAHY D-galactose specific lectin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ciw, resolution 2.70Å

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