Sandbox Reserved 489: Difference between revisions

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 </scene>3₁₀<scene name='Sandbox_Reserved_489/310heleices/1'> 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</scene> that forms the two similar lobes of renin.  <scene name='Sandbox_Reserved_489/Hydrophobichydrophillic/1'>Hydrophilic (blue) and hydrophobic (red) residues</scene> are located primarily on the outside and inside portions of renin respectively.  The most important structure is the <scene name='Sandbox_Reserved_489/Hydrophobicactivesite/1'>hydrophobic pocket</scene> located in the active site that allows substrate binding. 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>, a beta hairpin structure, 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/2'>Two asparagine residues</scene> at positions 14 and 75 can be glycosylated. The asparagine residue at postion 75 is glycosylated (2-(acetylamino)-2-deoxy-A-D-glucopyranose) in mature renin whereas the residue at postion 14 is not glycosylated.<ref>Margrane M. and the UnitProt consortium, '''Uniprot Knowledgebase: a hub of integrated protein data''', Database, 2012: bar009 (2011). Public Accession Number P00797 </ref>

The structure of recombinant human renin has been solved using X-ray diffraction at 2.5 angstrom resolution.<ref>PMID: 2493678</ref>