1bln: Difference between revisions

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[[Image:1bln.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_1bln|  PDB=1bln  |  SCENE=  }}  
{{STRUCTURE_1bln|  PDB=1bln  |  SCENE=  }}  


'''ANTI-P-GLYCOPROTEIN FAB MRK-16'''
===ANTI-P-GLYCOPROTEIN FAB MRK-16===




==Overview==
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Monoclonal antibody MRK-16 recognizes a discontinuous extracellular epitope on the multidrug resistance-associated ATP-binding cassette transporter, P-glycoprotein. The atomic basis for specificity of this antibody is of interest because of its potential as a modulator of P-glycoprotein activity. The crystal structure of Fab MRK-16 is reported to a resolution of 2.8 A. A structure for a portion of the epitope was derived by comparison to regions of solved structures with similar primary sequence. This has permitted a proposal for the mode of binding of the peptide epitope to the antibody, in which the peptide makes specific contacts with complementarity-determining regions H1, H2, and H3 from the heavy chain and L3 from the light chain. These interactions are consistent with epitope mapping studies and with the observation that MRK-16 is specific for human class I P-glycoprotein. This result identifies side chains in MRK-16 that would be amenable to alteration in antibody engineering experiments to derive improved multidrug resistance inhibitors for clinical use during chemotherapy. In particular, Arg-H97 contacts both Glu-746 and Asp-744 of the peptide, Arg-L96 contacts Asp-743, and Thr-H33 interacts with Thr-747. All of these epitope residues were implicated in mediating specificity by epitope mapping studies.
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{{ABSTRACT_PUBMED_9738009}}


==About this Structure==
==About this Structure==
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[[Category: Vasudevan, S.]]
[[Category: Vasudevan, S.]]
[[Category: Immunoglobulin]]
[[Category: Immunoglobulin]]
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