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{{STRUCTURE_1ce1|  PDB=1ce1  |  SCENE=  }}
===1.9A STRUCTURE OF THE THERAPEUTIC ANTIBODY CAMPATH-1H FAB IN COMPLEX WITH A SYNTHETIC PEPTIDE ANTIGEN===
{{ABSTRACT_PUBMED_10366506}}


==About this Structure==
==1.9A STRUCTURE OF THE THERAPEUTIC ANTIBODY CAMPATH-1H FAB IN COMPLEX WITH A SYNTHETIC PEPTIDE ANTIGEN==
[[1ce1]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE1 OCA].  
<StructureSection load='1ce1' size='340' side='right'caption='[[1ce1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ce1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CE1 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]] 1.9&#8491;</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=1ce1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ce1 OCA], [https://pdbe.org/1ce1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ce1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ce1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ce1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6PYX1_HUMAN Q6PYX1_HUMAN]
== 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/ce/1ce1_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=1ce1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CAMPATH-1 antibodies have a long and successful history in the treatment of leukaemia, autoimmune disease and transplant rejection. The first antibody to undergo "humanisation", CAMPATH-1H, permits treatment with limited patient anti-globulin response. It recognises the CD52 antigen which is a small glycosylphosphatidylinositol(GPI)-anchored protein expressed on lymphocytes and mediates cell depletion. We present the 1.9 A structure of the CAMPATH-1H Fab complexed [corrected] with an analogue of the antigenic determinant of CD52. Analysis of the CAMPATH-1H binding site reveals that in contrast to most antibodies CDR L3 plays a dominant role in antigen binding. Furthermore CDR H3, which is essential for effective antigen recognition in most antibodies, participates in only two main-chain interactions in CAMPATH-1H. The CAMPATH-1H binding site is highly basic; ionic interaction with the enthanolamine phosphate of the CD52 GPI anchor has long been hypothesised to be important in antigen binding. The structure reveals a number of important specific ionic interactions, including Lys53H but not Lys52bH as had previously been suggested. Prolonged treatment with CAMPATH-1H can lead to patient anti-idiotype responses which may be exacerbated by the unusually high number of basic residues in the antibody. This suggests that a strategy where redundant basic residues are replaced with neutral counterparts may be effective in further reducing the immunogenicity of this versatile and widely used antibody.


==Reference==
1.9 A structure of the therapeutic antibody CAMPATH-1H fab in complex with a synthetic peptide antigen.,James LC, Hale G, Waldmann H, Bloomer AC J Mol Biol. 1999 Jun 4;289(2):293-301. PMID:10366506<ref>PMID:10366506</ref>
<ref group="xtra">PMID:010366506</ref><references group="xtra"/><references/>
 
[[Category: Escherichia coli]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Bloomer, A C.]]
</div>
[[Category: Hale, G.]]
<div class="pdbe-citations 1ce1" style="background-color:#fffaf0;"></div>
[[Category: James, L C.]]
== References ==
[[Category: Waldmann, H.]]
<references/>
[[Category: Antibody]]
__TOC__
[[Category: Cd52]]
</StructureSection>
[[Category: Immune system]]
[[Category: Homo sapiens]]
[[Category: Therapeutic]]
[[Category: Large Structures]]
[[Category: Bloomer AC]]
[[Category: Hale G]]
[[Category: James LC]]
[[Category: Waldmann H]]
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