Sandbox Reserved 1661: Difference between revisions
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Anaïs Kembou (talk | contribs) No edit summary |
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LLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | LLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | ||
Somatotropin does not exist as a linear chain of amino acids, it twists and folds on itself, forming the '''secondary structure'''. The protein, made up of a single chain, consists of four antiparallel aligned <scene name='86/868194/Alpha-helice/2'>α-helices</scene> in an up-up-down-down manner <ref name="Endokrynologika Polska">DOI:10.5603/EP.2013.0009</ref> [https://doi.org/10.1016/j.ghir.2013.02.002]. The first helix starts at the 6th amino acid, which is a leucine and ends with the 37th amino acid proline. It is separated from the other three helices after the 37th position. The 38th and 39th amino acids, which are lysine and glutamic acid are spliced out of the protein and therefore disconnects the first helix from the second one. The second helix starts at position 72 till 92, the third from 106 till 128 and the fourth helix from 154 until 184. All helices are ampipathic with strong <scene name='86/868194/Hydrophobic_regions/1'>hydrophobic regions</scene>, especially helix 2 is very hydrophobic. The [https://en.wikipedia.org/wiki/Hydrophobic_effect#:~:text=Structures%20of%20water%2Dsoluble%20proteins,interact%20with%20surrounding%20water%20molecules. hydrophobic protein core] is usually tigthly packed and any mutations in the hidden positions lead to destablilization <ref name="pubMed">PMID:17584122</ref>. | Somatotropin does not exist as a linear chain of amino acids, it twists and folds on itself, forming the '''secondary structure'''. The protein, made up of a single chain, consists of four antiparallel aligned <scene name='86/868194/Alpha-helice/2'>α-helices</scene> in an up-up-down-down manner <ref name="Endokrynologika Polska">DOI:10.5603/EP.2013.0009</ref> [https://doi.org/10.1016/j.ghir.2013.02.002]. The first helix starts at the 6th amino acid, which is a leucine and ends with the 37th amino acid proline. It is separated from the other three helices after the 37th position. The 38th and 39th amino acids, which are lysine and glutamic acid are spliced out of the protein and therefore disconnects the first helix from the second one. The second helix starts at position 72 till 92, the third from 106 till 128 and the fourth helix from 154 until 184. All helices are ampipathic with strong <scene name='86/868194/Hydrophobic_regions/1'>hydrophobic regions</scene>, especially helix 2 is very hydrophobic. The [https://en.wikipedia.org/wiki/Hydrophobic_effect#:~:text=Structures%20of%20water%2Dsoluble%20proteins,interact%20with%20surrounding%20water%20molecules. hydrophobic protein core] is usually tigthly packed and any mutations in the hidden positions lead to destablilization <ref name="pubMed">PMID:17584122</ref>. | ||
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== HGH receptors and interactions == | == HGH receptors and interactions == | ||
The [https://en.wikipedia.org/wiki/Growth_hormone_receptor#:~:text=8%20External%20links-,Structure,GH%20binding%20protein%20(GHBP). GH membrane receptor (GHR)] is found on many cells and tissues with the exception of the brain, testicles and thymus. It is part of the [[https://en.wikipedia.org/wiki/Type_I_cytokine_receptor class I cytokine receptor family] [https://doi.org/10.1016/j.ygcen.2017.07.028 ]. The nature of this receptor is not fully understood, but it seems that it may be present in different forms due to different post-translational changes that may occur in a single protein.<ref name="m/s"> Le Cam, A. (1993), Mode d’action de l’hormone de croissance. médecine/sciences, 12:1352-61.[http://www.ipubli.inserm.fr/bitstream/handle/10608/2863/MS_1993_12_1352.pdf?sequence=1]</ref> | The [https://en.wikipedia.org/wiki/Growth_hormone_receptor#:~:text=8%20External%20links-,Structure,GH%20binding%20protein%20(GHBP). GH membrane receptor (GHR)] is found on many cells and tissues with the exception of the brain, testicles and thymus. It is part of the [[https://en.wikipedia.org/wiki/Type_I_cytokine_receptor class I cytokine receptor family] [https://doi.org/10.1016/j.ygcen.2017.07.028 ]. The nature of this receptor is not fully understood, but it seems that it may be present in different forms due to different post-translational changes that may occur in a single protein.<ref name="m/s"> Le Cam, A. (1993), Mode d’action de l’hormone de croissance. médecine/sciences, 12:1352-61.[http://www.ipubli.inserm.fr/bitstream/handle/10608/2863/MS_1993_12_1352.pdf?sequence=1]</ref> | ||
