Extracellular domain structures from calcium-sensing and GABA(B) receptors

Published on July 31, 2019   36 min
0:00
My name is Qing Fan. I'm from Colombia University. The research in my lab involves the structural studies of class C G-protein coupled receptors.
0:12
GPCRs are divided into different classes based on the sequence homology of their trans-membrane domains. Most GPCRs such as rhodopsin and Beta-2 adrenergic receptor belong to class A. These receptors contain a seven helix trans-membrane domain and can function as monomers. The ligand binding site of the class A receptors is located within the trans-membrane domain. Landmark studies led by Dr. Kodaka's group revealed that agonist binding directly induces conformational changes among the trans-membrane helices for receptor activation. Class C GPCRs mediate a number of key biological phenomena including excitatory and inhibitory neurotransmission, calcium homeostasis, and taste. Unlike the class A receptors, the class GPCRs are characterized by a large extracellular domain. In addition to the canonical seven helix trans-membrane domain, this extracellular domain is 500-600 amino acids long and contains the orthosteric ligand binding site. Another unique feature of the class C receptors is that they require dimerization for function. While metabotropic glutamate receptors and calcium sensing receptor function as disulfide-linked homodimers, GABA B receptor and taste receptors are obligatory heterodimers. Our goal is to use structural methods to probe the signal transduction mechanisms of class C receptors and GPCR dimers in general. Specifically, we're focusing on human GABA B receptor and human calcium sensing receptor.
Hide

Extracellular domain structures from calcium-sensing and GABA(B) receptors

Embed in course/own notes