Sandbox Reserved 1661: Difference between revisions
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Anaïs Kembou (talk | contribs) No edit summary |
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The protein has two different binding sites: both located at the ends of the protein, the N-terminus as well as the C-terminus. | The protein has two different binding sites: both located at the ends of the protein, the N-terminus as well as the C-terminus. | ||
The GH consists of two hydrophobic cores, one is composed of Trp104 (hGH-receptor1), Trp169(hGH-receptor1), Pro61 (hGH), Phe176(hGH) and Ile176(hGH). Especially Pro61 is important, it is involved in the formation of the ative conformation of hydrophobic core amino acids and interacting with other hydrophobic core amino acids within 5Å. A mutation in this point leads to a decrease of biological and receptor binding activity. The other one is composed of two pairs of interaction between Trp76 (hGH-receptor1) and Pro48 (hGH) and between Pro106 (hGH-receptor1) and Leu45 (hGH). <ref name="pubMed">PMID:17584122</ref> | The GH consists of two hydrophobic cores, one is composed of Trp104 (hGH-receptor1), Trp169(hGH-receptor1), Pro61 (hGH), Phe176(hGH) and Ile176(hGH). Especially Pro61 is important, it is involved in the formation of the ative conformation of hydrophobic core amino acids and interacting with other hydrophobic core amino acids within 5Å. A mutation in this point leads to a decrease of biological and receptor binding activity. The other one is composed of two pairs of interaction between Trp76 (hGH-receptor1) and Pro48 (hGH) and between Pro106 (hGH-receptor1) and Leu45 (hGH). <ref name="pubMed">PMID:17584122</ref> | ||
<scene name='86/868194/Test/1'>Test</scene> | |||
