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Atomic-level mapping of antibody epitopes on a GPCR.


ABSTRACT: Epitopes that define the immunodominant regions of conformationally complex integral membrane proteins have been difficult to reliably delineate. Here, a high-throughput approach termed shotgun mutagenesis was used to map the binding epitopes of five different monoclonal antibodies targeting the GPCR CCR5. The amino acids, and in some cases the atoms, that comprise the critical contact points of each epitope were identified, defining the immunodominant structures of this GPCR and their physicochemistry.

SUBMITTER: Paes C 

PROVIDER: S-EPMC2943208 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature

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Atomic-level mapping of antibody epitopes on a GPCR.

Paes Cheryl C   Ingalls Jada J   Kampani Karan K   Sulli Chidananda C   Kakkar Esha E   Murray Meredith M   Kotelnikov Valery V   Greene Tiffani A TA   Rucker Joseph B JB   Doranz Benjamin J BJ  

Journal of the American Chemical Society 20090501 20


Epitopes that define the immunodominant regions of conformationally complex integral membrane proteins have been difficult to reliably delineate. Here, a high-throughput approach termed shotgun mutagenesis was used to map the binding epitopes of five different monoclonal antibodies targeting the GPCR CCR5. The amino acids, and in some cases the atoms, that comprise the critical contact points of each epitope were identified, defining the immunodominant structures of this GPCR and their physicoch  ...[more]

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