1uz8: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1uz8.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1uz8", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1uz8|  PDB=1uz8  |  SCENE=  }}
'''ANTI-LEWIS X FAB FRAGMENT IN COMPLEX WITH LEWIS X'''


==anti-Lewis X Fab fragment in complex with Lewis X==
<StructureSection load='1uz8' size='340' side='right'caption='[[1uz8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1uz8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UZ8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAG:BETA-METHYL-N-ACETYL-D-GLUCOSAMINE'>MAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uz8 OCA], [https://pdbe.org/1uz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uz8 RCSB], [https://www.ebi.ac.uk/pdbsum/1uz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uz8 ProSAT]</span></td></tr>
</table>
== 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/uz/1uz8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1uz8 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Lewis X trisaccharide is pivotal in mediating specific cell-cell interactions. Monoclonal antibody 291-2G3-A, which was generated from mice infected with schistosomes, has been shown to recognize the Lewis X trisaccharide. Here we describe the structure of the Fab fragment of 291-2G3-A, with Lewis X, to 1.8 A resolution. The crystallographic analysis revealed that the antigen binding site is a rather shallow binding pocket, and residues from all six complementary determining regions of the antibody contact all sugar residues. The high specificity of the binding pocket does not result in high affinity; the K(D) determined by isothermal calorimetry is 11 microM. However, this affinity is in the same range as for other sugar-antibody complexes. The detailed understanding of the antibody-Lewis X interaction revealed by the crystal structure may be helpful in the design of better diagnostic tools for schistosomiasis and for studying Lewis X-mediated cell-cell interactions by antibody interference.


==Overview==
Structure of an anti-Lewis X Fab fragment in complex with its Lewis X antigen.,van Roon AM, Pannu NS, de Vrind JP, van der Marel GA, van Boom JH, Hokke CH, Deelder AM, Abrahams JP Structure. 2004 Jul;12(7):1227-36. PMID:15242599<ref>PMID:15242599</ref>
The Lewis X trisaccharide is pivotal in mediating specific cell-cell interactions. Monoclonal antibody 291-2G3-A, which was generated from mice infected with schistosomes, has been shown to recognize the Lewis X trisaccharide. Here we describe the structure of the Fab fragment of 291-2G3-A, with Lewis X, to 1.8 A resolution. The crystallographic analysis revealed that the antigen binding site is a rather shallow binding pocket, and residues from all six complementary determining regions of the antibody contact all sugar residues. The high specificity of the binding pocket does not result in high affinity; the K(D) determined by isothermal calorimetry is 11 microM. However, this affinity is in the same range as for other sugar-antibody complexes. The detailed understanding of the antibody-Lewis X interaction revealed by the crystal structure may be helpful in the design of better diagnostic tools for schistosomiasis and for studying Lewis X-mediated cell-cell interactions by antibody interference.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1UZ8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UZ8 OCA].
</div>
<div class="pdbe-citations 1uz8" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of an anti-Lewis X Fab fragment in complex with its Lewis X antigen., van Roon AM, Pannu NS, de Vrind JP, van der Marel GA, van Boom JH, Hokke CH, Deelder AM, Abrahams JP, Structure. 2004 Jul;12(7):1227-36. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15242599 15242599]
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Abrahams JP]]
[[Category: Abrahams, J P.]]
[[Category: De Vrind JPM]]
[[Category: Boom, J H.Van.]]
[[Category: Deelder AM]]
[[Category: Deelder, A M.]]
[[Category: Hokke CH]]
[[Category: Hokke, C H.]]
[[Category: Pannu NS]]
[[Category: Marel, G A.Van Der.]]
[[Category: Van Boom JH]]
[[Category: Pannu, N S.]]
[[Category: Van Der marel GA]]
[[Category: Roon, A M.M Van.]]
[[Category: Van Roon AMM]]
[[Category: Vrind, J P.M De.]]
[[Category: Anti-carbohydrate]]
[[Category: Antibody]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:53:35 2008''

Latest revision as of 07:57, 17 October 2024

anti-Lewis X Fab fragment in complex with Lewis Xanti-Lewis X Fab fragment in complex with Lewis X

Structural highlights

1uz8 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

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

Publication Abstract from PubMed

The Lewis X trisaccharide is pivotal in mediating specific cell-cell interactions. Monoclonal antibody 291-2G3-A, which was generated from mice infected with schistosomes, has been shown to recognize the Lewis X trisaccharide. Here we describe the structure of the Fab fragment of 291-2G3-A, with Lewis X, to 1.8 A resolution. The crystallographic analysis revealed that the antigen binding site is a rather shallow binding pocket, and residues from all six complementary determining regions of the antibody contact all sugar residues. The high specificity of the binding pocket does not result in high affinity; the K(D) determined by isothermal calorimetry is 11 microM. However, this affinity is in the same range as for other sugar-antibody complexes. The detailed understanding of the antibody-Lewis X interaction revealed by the crystal structure may be helpful in the design of better diagnostic tools for schistosomiasis and for studying Lewis X-mediated cell-cell interactions by antibody interference.

Structure of an anti-Lewis X Fab fragment in complex with its Lewis X antigen.,van Roon AM, Pannu NS, de Vrind JP, van der Marel GA, van Boom JH, Hokke CH, Deelder AM, Abrahams JP Structure. 2004 Jul;12(7):1227-36. PMID:15242599[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ van Roon AM, Pannu NS, de Vrind JP, van der Marel GA, van Boom JH, Hokke CH, Deelder AM, Abrahams JP. Structure of an anti-Lewis X Fab fragment in complex with its Lewis X antigen. Structure. 2004 Jul;12(7):1227-36. PMID:15242599 doi:10.1016/j.str.2004.05.008

1uz8, resolution 1.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1uz8&oldid=4191276"