Sandbox Reserved 1120: Difference between revisions
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<tr><td colspan='2'>The SRY protein is a 204 residues-long monomeric polypeptide. It is encoded by the SRY gene and is involved in the sex determination in mammals by being responsible for the gonadogenesis and so the male sexual development. It is the HMG-box that gives to the protein its ability to bind DNA by its minor groove. <ref>PMID: 9626701</ref></td></tr> | <tr><td colspan='2'>The SRY protein is a 204 residues-long monomeric polypeptide. It is encoded by the SRY gene and is involved in the sex determination in mammals by being responsible for the gonadogenesis and so the male sexual development. It is the HMG-box that gives to the protein its ability to bind DNA by its minor groove. <ref name ="Tang">PMID: 9626701</ref></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hrz|1hrz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hrz|1hrz]]</td></tr> | ||
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*<scene name='71/719861/Short_arm_22a/1'>Short arm (22Å)</scene> | *<scene name='71/719861/Short_arm_22a/1'>Short arm (22Å)</scene> | ||
The interaction between the HMG-Box and DNA is specific and stable. It is mostly hydrophobic. It permits the DNA to bend of DNA (≈75°). Only one molecule of water interfaces the Box and the DNA. The complex is stabilized by salt bridges between positively charged residues of the HMG domain and negatively charged phosphates<ref | The interaction between the HMG-Box and DNA is specific and stable. It is mostly hydrophobic. It permits the DNA to bend of DNA (≈75°). Only one molecule of water interfaces the Box and the DNA. The complex is stabilized by salt bridges between positively charged residues of the HMG domain and negatively charged phosphates<ref name="Tang" />. | ||
[[Image:HHMG-bitmap.png|thumb|alt=Image bitmap|Linear structure of hHMG domain]] | [[Image:HHMG-bitmap.png|thumb|alt=Image bitmap|Linear structure of hHMG domain]] | ||
