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| | <StructureSection load='1bey' size='340' side='right'caption='[[1bey]], [[Resolution|resolution]] 3.25Å' scene=''> | | <StructureSection load='1bey' size='340' side='right'caption='[[1bey]], [[Resolution|resolution]] 3.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bey]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BEY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bey]] is a 2 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=1BEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BEY FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bey OCA], [http://pdbe.org/1bey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bey RCSB], [http://www.ebi.ac.uk/pdbsum/1bey PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bey ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.25Å</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=1bey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bey OCA], [https://pdbe.org/1bey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bey RCSB], [https://www.ebi.ac.uk/pdbsum/1bey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bey ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6GMX0_HUMAN Q6GMX0_HUMAN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bloomer, A C]] | + | [[Category: Bloomer AC]] |
| - | [[Category: Cheetham, G M.T]] | + | [[Category: Cheetham GMT]] |
| - | [[Category: Hale, G]] | + | [[Category: Hale G]] |
| - | [[Category: Waldmann, H]] | + | [[Category: Waldmann H]] |
| - | [[Category: Antibody]]
| + | |
| - | [[Category: Campath-1h]]
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| - | [[Category: Cd52]]
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| - | [[Category: Fab]]
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| Structural highlights
Function
Q6GMX0_HUMAN
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 CAMPATH-1 family of antibodies are able systematically to lyse human lymphocytes with human complement by targeting the small cell-surface glycoprotein CD52, commonly called the CAMPATH-1 antigen. These antibodies have been used clinically for several years, providing therapy for patients with a variety of immunologically mediated diseases. We report here the first X-ray crystallographic analyses of a Fab fragment from a rat antibody, the original therapeutic monoclonal CAMPATH-1G and its humanized counterpart CAMPATH-1H, into which the six complementarity-determining regions of the rat antibody have been introduced. These structures have been refined at 2.6 A and 3.25 A resolution, respectively. The VL domains of adjacent molecules of CAMPATH-1H form a symmetric dimer within the crystals with an inter-molecular extended beta-sheet as seen in light chain dimers of the kappa class. Crystals of CAMPATH-1G have translational pseudo-symmetry. Within the antibody-combining sites, which are dominated by the protrusion of LysH52b and LysH53 from hypervariable loop H2, the charge distribution and overall integrity are highly conserved, but large changes in the position of loop H1 are observed and an altered conformation of loop H2. The major determinants of this are framework residues H71 and H24, whose identity differs in these two antibodies. These structures provide a detailed structural insight into the transplantation of an intact antibody-combining site between a rodent and a human framework, and provide an increased understanding of the specificity and antigen affinity of this pair of CAMPATH-1 antibodies for CD52. This study forms the structural basis for future modification and design of more effective antibodies to this important antigen.
Crystal structures of a rat anti-CD52 (CAMPATH-1) therapeutic antibody Fab fragment and its humanized counterpart.,Cheetham GM, Hale G, Waldmann H, Bloomer AC J Mol Biol. 1998 Nov 20;284(1):85-99. PMID:9811544[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cheetham GM, Hale G, Waldmann H, Bloomer AC. Crystal structures of a rat anti-CD52 (CAMPATH-1) therapeutic antibody Fab fragment and its humanized counterpart. J Mol Biol. 1998 Nov 20;284(1):85-99. PMID:9811544 doi:10.1006/jmbi.1998.2157
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