1bey: Difference between revisions
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[[Image:1bey.jpg|left|200px]] | [[Image:1bey.jpg|left|200px]] | ||
'''ANTIBODY TO CAMPATH-1H HUMANIZED FAB''' | {{Structure | ||
|PDB= 1bey |SIZE=350|CAPTION= <scene name='initialview01'>1bey</scene>, resolution 3.25Å | |||
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|LIGAND= | |||
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'''ANTIBODY TO CAMPATH-1H HUMANIZED FAB''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BEY is a [ | 1BEY is a [[Protein complex]] structure of sequences 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]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9811544 9811544] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: fab]] | [[Category: fab]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:09 2008'' | ||
Revision as of 11:10, 20 March 2008
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ANTIBODY TO CAMPATH-1H HUMANIZED FAB
OverviewOverview
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.
About this StructureAbout this Structure
1BEY is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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