Renin: Difference between revisions
No edit summary |
No edit summary |
||
| Line 19: | Line 19: | ||
==Structure== | ==Structure== | ||
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 29 <scene name='Sandbox_Reserved_489/Betasheetscolors/1'> antiparallel β sheets</scene>, 3 <scene name='Sandbox_Reserved_489/Betabridges/1'> β bridges</scene>, 4 <scene name='Sandbox_Reserved_489/Alphahelixes/1'> α helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'> 2 </scene>3<sub>10</sub><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 antiparallel <scene name='Sandbox_Reserved_489/Betasheetspiral/1'> β 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 β hairpin structure, 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 29 <scene name='Sandbox_Reserved_489/Betasheetscolors/1'> antiparallel β sheets</scene>, 3 <scene name='Sandbox_Reserved_489/Betabridges/1'> β bridges</scene>, 4 <scene name='Sandbox_Reserved_489/Alphahelixes/1'> α helices</scene>, <scene name='Sandbox_Reserved_489/310heleices/1'> 2 </scene>3<sub>10</sub><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 antiparallel <scene name='Sandbox_Reserved_489/Betasheetspiral/1'> β 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 β hairpin structure, that open and closes to uncover or cover the active site. | ||
| Line 52: | Line 51: | ||
Familial juvenile hyperuricemic nephropathy type 2 is also caused by defects in the renin gene. Familial juvenile hyperuricemic nephropathy type 2 is characterized by slowly progressive renal failure and anemia. The autosomal dominant disorder is caused by a deletion of leucine 16 or a mutation of leucine 16 to arginine. The mutations effect the hydrophobicity of the signal sequence and disrupt the proper transport of preprorenin into the endoplasmic reticulum and thus effecting prerenin processing. The mutatnt proteins are toxic and reduce the viability of renin expressing cells, eventually causing renal failure.<ref>PMID:19664745</ref> | Familial juvenile hyperuricemic nephropathy type 2 is also caused by defects in the renin gene. Familial juvenile hyperuricemic nephropathy type 2 is characterized by slowly progressive renal failure and anemia. The autosomal dominant disorder is caused by a deletion of leucine 16 or a mutation of leucine 16 to arginine. The mutations effect the hydrophobicity of the signal sequence and disrupt the proper transport of preprorenin into the endoplasmic reticulum and thus effecting prerenin processing. The mutatnt proteins are toxic and reduce the viability of renin expressing cells, eventually causing renal failure.<ref>PMID:19664745</ref> | ||
</StructureSection> | |||
__NOTOC__ | |||
==3D structures of renin== | ==3D structures of renin== | ||