Sandbox Reserved 489: Difference between revisions
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The precursor of renin is a 406 amino acid residue protein. <scene name='Sandbox_Reserved_489/Signal_domain/1'>Residues 1-23</scene> are a signal peptide sequence and residues 24-66 are cleaved to produce the mature 340 amino acid residue <scene name='Sandbox_Reserved_489/Mature_renin/1'>mature renin</scene>. The secondary structural elements of renin include <scene name='Sandbox_Reserved_489/Betasheetscolors/1'>29 antiparallel beta sheets</scene>, <scene name='Sandbox_Reserved_489/Betabridges/1'>3 beta bridges</scene>, <scene name='Sandbox_Reserved_489/Alphahelixes/1'>4 alpha helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'>2 3-10 helices</scene>, and <scene name='Sandbox_Reserved_489/Turns/1'>18 turns</scene>. The most impressive structural feature of renin is the <scene name='Sandbox_Reserved_489/Betasheetspiral/1'>antiparallel beta sheet elongated spiral barrel</scene>. <scene name='Sandbox_Reserved_489/Hydrophobichydrophillic/1'>Hydrophilic and hydrophobic residues</scene> are practically evenly distributed throughout renin. The alternating hydrophilic and hydrophobic residues most likely assist in folding of the unique spiral structure. The active site of renin contains two essential <scene name='Sandbox_Reserved_489/Activesiteasps2/2'>aspartate residues</scene>. Renin has <scene name='Sandbox_Reserved_489/Catalyticmotifs/1'>two catalytic motifs</scene> after each of the two aspartate residues. Renin also uses a <scene name='Sandbox_Reserved_489/Activesiteflap/1'>active site flap</scene> that open and closes to uncover or cover the active site. | The precursor of renin is a 406 amino acid residue protein. <scene name='Sandbox_Reserved_489/Signal_domain/1'>Residues 1-23</scene> are a signal peptide sequence and residues 24-66 are cleaved to produce the mature 340 amino acid residue <scene name='Sandbox_Reserved_489/Mature_renin/1'>mature renin</scene>. The secondary structural elements of renin include <scene name='Sandbox_Reserved_489/Betasheetscolors/1'>29 antiparallel beta sheets</scene>, <scene name='Sandbox_Reserved_489/Betabridges/1'>3 beta bridges</scene>, <scene name='Sandbox_Reserved_489/Alphahelixes/1'>4 alpha helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'>2 3-10 helices</scene>, and <scene name='Sandbox_Reserved_489/Turns/1'>18 turns</scene>. The most impressive structural feature of renin is the <scene name='Sandbox_Reserved_489/Betasheetspiral/1'>antiparallel beta sheet elongated spiral barrel</scene>. <scene name='Sandbox_Reserved_489/Hydrophobichydrophillic/1'>Hydrophilic and hydrophobic residues</scene> are practically evenly distributed throughout renin. The alternating hydrophilic and hydrophobic residues most likely assist in folding of the unique spiral structure. The active site of renin contains two essential <scene name='Sandbox_Reserved_489/Activesiteasps2/2'>aspartate residues</scene>. Renin has <scene name='Sandbox_Reserved_489/Catalyticmotifs/1'>two catalytic motifs</scene> after each of the two aspartate residues. Renin also uses a <scene name='Sandbox_Reserved_489/Activesiteflap/1'>active site flap</scene> that open and closes to uncover or cover the active site. | ||
Post translational modifications of renin include; precursor cleavage of propetide to produce active mature renin, disulfide bond formation, and glycosylation of certain residues. Disulfide bonds are form to connect serine residues <scene name='Sandbox_Reserved_489/Disulfidebond1/1'>51 to 58</scene>, <scene name='Sandbox_Reserved_489/Disulfidebond2/1'>217 to 221</scene>, and <scene name='Sandbox_Reserved_489/Disulfidebond3/1'>259 to 296</scene>. <scene name='Sandbox_Reserved_489/Glycosylated/ | Post translational modifications of renin include; precursor cleavage of propetide to produce active mature renin, disulfide bond formation, and glycosylation of certain residues. Disulfide bonds are form to connect serine residues <scene name='Sandbox_Reserved_489/Disulfidebond1/1'>51 to 58</scene>, <scene name='Sandbox_Reserved_489/Disulfidebond2/1'>217 to 221</scene>, and <scene name='Sandbox_Reserved_489/Disulfidebond3/1'>259 to 296</scene>. <scene name='Sandbox_Reserved_489/Glycosylated/2'>Two asparagine residues</scene> at positions 14 and 75 can be glycosylated. The asparagine residue at postion 75 is glycosylated with 2-(acetylamino)-2-deoxy-A-D-glucopyranose in mature renin whereas the residue at postion 14 is not glycosylated. | ||
==Function== | ==Function== | ||
