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| - | [[Image:1ce1.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ce1| PDB=1ce1 | SCENE= }} | | {{STRUCTURE_1ce1| PDB=1ce1 | SCENE= }} |
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| - | '''1.9A STRUCTURE OF THE THERAPEUTIC ANTIBODY CAMPATH-1H FAB IN COMPLEX WITH A SYNTHETIC PEPTIDE ANTIGEN'''
| + | ===1.9A STRUCTURE OF THE THERAPEUTIC ANTIBODY CAMPATH-1H FAB IN COMPLEX WITH A SYNTHETIC PEPTIDE ANTIGEN=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10366506}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10366506 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10366506}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Cd52]] | | [[Category: Cd52]] |
| | [[Category: Therapeutic]] | | [[Category: Therapeutic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:37:27 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:36:53 2008'' |
Revision as of 17:36, 30 June 2008
Template:STRUCTURE 1ce1
1.9A STRUCTURE OF THE THERAPEUTIC ANTIBODY CAMPATH-1H FAB IN COMPLEX WITH A SYNTHETIC PEPTIDE ANTIGEN
Template:ABSTRACT PUBMED 10366506
About this Structure
1CE1 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
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
Page seeded by OCA on Mon Jun 30 20:36:53 2008
