1. A monoclonal antibody for G protein-coupled receptor crystallography
- Author
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Asna Masood, Daniel K. Rohrer, Peter Day, Søren G. F. Rasmussen, William I. Weis, Tong Sun Kobilka, Brian K. Kobilka, Xiao-Jie Yao, Juan Jose Fung, Charles Parnot, and Hee Jung Choi
- Subjects
medicine.drug_class ,Blotting, Western ,Molecular Sequence Data ,Monoclonal antibody ,Biochemistry ,Epitope ,Receptors, G-Protein-Coupled ,Antigen-Antibody Reactions ,Epitopes ,Immunoglobulin Fab Fragments ,Mice ,Protein structure ,medicine ,Animals ,Humans ,Amino Acid Sequence ,Receptor ,Molecular Biology ,Peptide sequence ,G protein-coupled receptor ,Fluorescent Dyes ,Crystallography ,biology ,Rhodamines ,Vaccination ,Antibodies, Monoclonal ,Cell Biology ,Recombinant Proteins ,Protein Structure, Tertiary ,biology.protein ,Receptors, Adrenergic, beta-2 ,Antibody ,Signal transduction ,Crystallization ,Biotechnology - Abstract
G protein-coupled receptors (GPCRs) constitute the largest family of signaling proteins in mammals, mediating responses to hormones, neurotransmitters, and senses of sight, smell and taste. Mechanistic insight into GPCR signal transduction is limited by a paucity of high-resolution structural information. We describe the generation of a monoclonal antibody that recognizes the third intracellular loop (IL3) of the native human beta(2) adrenergic (beta(2)AR) receptor; this antibody was critical for acquiring diffraction-quality crystals.
- Published
- 2007