1cu4: Difference between revisions
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'''CRYSTAL STRUCTURE OF THE ANTI-PRION FAB 3F4 IN COMPLEX WITH ITS PEPTIDE EPITOPE''' | {{Structure | ||
|PDB= 1cu4 |SIZE=350|CAPTION= <scene name='initialview01'>1cu4</scene>, resolution 2.9Å | |||
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'''CRYSTAL STRUCTURE OF THE ANTI-PRION FAB 3F4 IN COMPLEX WITH ITS PEPTIDE EPITOPE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CU4 is a [ | 1CU4 is a [[Protein complex]] structure of sequences 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=1CU4 OCA]. | ||
==Reference== | ==Reference== | ||
Antibody binding defines a structure for an epitope that participates in the PrPC-->PrPSc conformational change., Kanyo ZF, Pan KM, Williamson RA, Burton DR, Prusiner SB, Fletterick RJ, Cohen FE, J Mol Biol. 1999 Nov 5;293(4):855-63. PMID:[http:// | Antibody binding defines a structure for an epitope that participates in the PrPC-->PrPSc conformational change., Kanyo ZF, Pan KM, Williamson RA, Burton DR, Prusiner SB, Fletterick RJ, Cohen FE, J Mol Biol. 1999 Nov 5;293(4):855-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10543972 10543972] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: immunoglobulin fold]] | [[Category: immunoglobulin fold]] | ||
''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 10:28:54 2008'' | ||
Revision as of 11:28, 20 March 2008
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CRYSTAL STRUCTURE OF THE ANTI-PRION FAB 3F4 IN COMPLEX WITH ITS PEPTIDE EPITOPE
OverviewOverview
The X-ray crystallographic structures of the anti-Syrian hamster prion protein (SHaPrP) monoclonal Fab 3F4 alone, as well as the complex with its cognate peptide epitope (SHaPrP 104-113), have been determined to atomic resolution. The conformation of the decapeptide is an Omega-loop. There are substantial alterations in the antibody combining region upon epitope binding. The peptide binds in a U-shaped groove on the Fab surface, with the two specificity determinants, Met109 and Met112, penetrating deeply into separate hydrophobic cavities formed by the heavy and light chain complementarity-determining regions. In addition to the numerous contacts between the Fab and the peptide, two intrapeptide hydrogen bonds are observed, perhaps indicating the structure bound to the Fab exists transiently in solution. This provides the first structural information on a portion of the PrP N-terminal region observed to be flexible in the NMR studies of SHPrP 90-231, SHaPrP 29-231 and mouse PrP 23-231. Antibody characterization of the antigenic surfaces of PrPC and PrPSc identifies this flexible region as a component of the conformational rearrangement that is an essential feature of prion disease.
About this StructureAbout this Structure
1CU4 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Antibody binding defines a structure for an epitope that participates in the PrPC-->PrPSc conformational change., Kanyo ZF, Pan KM, Williamson RA, Burton DR, Prusiner SB, Fletterick RJ, Cohen FE, J Mol Biol. 1999 Nov 5;293(4):855-63. PMID:10543972
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