期刊
RELAXIN AND RELATED PEPTIDES: FIFTH INTERNATIONAL CONFERENCE
卷 1160, 期 -, 页码 45-53出版社
WILEY-BLACKWELL
DOI: 10.1111/j.1749-6632.2009.03837.x
关键词
insulin; IGF-I; IGF-II; relaxin; INSL; RXFP; RTK; GPCR; LGR; allosterism; negative cooperativity
类别
资金
- Dainsh Ministry of Science, Technology and Innovation
- Novo Nordisk's CORA
The insulin/relaxin superfamily of peptide hormones comprises 10 members in humans. The three members of the insulin-related subgroup bind to receptor tyrosine kinases (RTKs), while four of the seven members of the relaxin-like subgroup are now known to bind to G-protein-coupled receptors (GPCRs), the so-called relaxin family peptide receptors (RXFPs). Both systems have a long evolutionary history and play a critical role in fundamental biological processes, such as metabolism, growth, survival and longevity, and reproduction. The structural biology and ligand-binding kinetics of the insulin and insulin-like growth factor I receptors have been studied in great detail, culminating in the recent crystal structure of the insulin receptor extracellular domain. Some of the fundamental properties of these receptors, including constitutive dimerization and negative cooperativity, have recently been shown to extend to other RTKs and GPCRs, including RXFPs, confirming kinetic observations made over 30 years ago.
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