Fig. 5.
Fig. 5. Comparison of D4βc with the membrane-proximal domain of GHR. / D4βc and domain 2 of the subunit of the GHR, which interacts with the helix A/helix C face of GH, were aligned structurally via their core residues and are shown as surface representations using the program InsightII (MSI, San Diego, CA). The hydrophobic-aromatic patch, H2, of D4βc and the location of GHR that interacts with the opposing receptor molecule are indicated by green surfaces. The red surfaces of D4βc indicate the residues required for affinity-conversion, and the blue surfaces of GHR indicate the region known to interact with GH.

Comparison of D4βc with the membrane-proximal domain of GHR.

D4βc and domain 2 of the subunit of the GHR, which interacts with the helix A/helix C face of GH, were aligned structurally via their core residues and are shown as surface representations using the program InsightII (MSI, San Diego, CA). The hydrophobic-aromatic patch, H2, of D4βc and the location of GHR that interacts with the opposing receptor molecule are indicated by green surfaces. The red surfaces of D4βc indicate the residues required for affinity-conversion, and the blue surfaces of GHR indicate the region known to interact with GH.

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