Article
Structure of a phage display-derived variant of human growth hormone complexed to two copies of the extracellular domain of its receptor: evidence for strong structural coupling between receptor binding sites.
Journal of molecular biology - 15 Feb 2002
Schiffer Celia, Ultsch Mark, Walsh Scott, Somers William, de Vos Abraham M, Kossiakoff Anthony
Abstract excerpt
The structure of the ternary complex between the phage display- optimized, high-affinity Site 1 variant of human growth hormone (hGH) and two copies of the extracellular domain (ECD) of the hGH receptor (hGHR) has been determined at 2.6 A resolution. There are widespread and significant structural differences compared to the wild-type ternary hGH hGHR complex. The hGH variant (hGH(v)) contains 15 Site 1 mutations...
Topics
- Binding Sites
- Crystallography, X-Ray
- Dimerization
- Human Growth Hormone
- Humans
- Hydrogen Bonding
- Hydrophobic and Hydrophilic Interactions
- Models, Molecular
- Mutation
- Peptide Library