Sandbox Reserved 347: Difference between revisions

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==Structure==

Renin belongs in a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref> Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. <ref name="hypertension"/> Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.<ref name="cloning">PMID:9556453</ref>

Renin belongs in a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref> Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. <ref name="hypertension"/> Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.<ref name="cloning">PMID:9556453</ref> Uniquely from other proteases, Renin has two β-carboxyl groups of Asp32 and Asp215 which protrude from each of the two lobes into the active site and has a large flap covering the <scene name='Sandbox_Reserved_347/Ligand/1'>Active site</scene>.<ref name= "Structure">PMID:2666611</ref>

~~==Biochemistry==~~

~~[[Image:Man pic.png|thumb|left|Renin-Angiotensin-Aldosterone System]]~~

~~Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref>~~

~~<scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene>~~

*Renin is found in the blood stream where it breaks down angiotensinogen, which is secreted from the liver, into angiotensin I.

*Angiotensin I is then cleaved in the lungs by angiotensin converting enzymes (ACE) into angiotensin II.

==Function==

Renin plays a key role in the Renin-Angiotension sysmtem (RAS). It is essential in facilitating the conversion of angiotension to angiotension II, which is the active component of the system.<ref name="review">DOI: 10.1146/annurev.ph.40.030178.002113</ref> This system is responsible for the regulation of blood pressure, stimulation of the secretion of aldosterone which effects the salt and water balance.<ref name="review"/>

[[Image:Man pic.png|thumb|left|Renin-Angiotensin-Aldosterone System]]

Renin plays a key role in the Renin-Angiotension sysmtem (RAS). It is essential in facilitating the conversion of angiotension to angiotension II, which is the active component of the RAS system.<ref name="review">DOI: 10.1146/annurev.ph.40.030178.002113</ref> This system is responsible for the regulation of blood pressure, stimulation of the secretion of aldosterone which effects the salt and water balance.<ref name="review"/>

*Angiotensinogen is released into the bloodstream by the liver.

*Likewise, Renin is secreted by the kidneys into the bloodstream where is meets with angiotensinogen.

*Once united, angiotensinogen form the decapeptide angiotensin (ANG) I.

*ANG I is then activated by Angiotensin converting enzyme (ACE) to form the octapeptide ANG II.

*ANG II then acts on specific receptors such as ones responsible for vasoconstriction or the release of aldosterone from the adrenal cortex. <ref name="renin review"> doi: 10.1152/physrev.00036.2005

</ref>

Sandbox Reserved 347: Difference between revisions

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@@ Line 11: / Line 11: @@
 ==Structure==
-Renin belongs in a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref>  Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. <ref name="hypertension"/> Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.<ref name="cloning">PMID:9556453</ref>
+Renin belongs in a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. <ref name="3D">K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". ''Hypertension''. 1985;7:3-12</ref>  Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. <ref name="hypertension"/> Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.<ref name="cloning">PMID:9556453</ref> Uniquely from other proteases, Renin has two β-carboxyl groups of Asp32 and Asp215 which protrude from each of the two lobes into the active site and has a large flap covering the <scene name='Sandbox_Reserved_347/Ligand/1'>Active site</scene>.<ref name= "Structure">PMID:2666611</ref>
-==Biochemistry==
-[[Image:Man pic.png|thumb|left|Renin-Angiotensin-Aldosterone System]]
-Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref>
 <Structure load='2iko' size='500' frame='true' align='right' caption='Renin active site' scene='Sandbox_Reserved_347/Ligand/1' />
-<scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene>
-*Renin is found in the blood stream where it breaks down angiotensinogen, which is secreted from the liver, into angiotensin I.
-*Angiotensin I is then cleaved in the lungs by angiotensin converting enzymes (ACE) into angiotensin II.
 ==Function==
-Renin plays a key role in the Renin-Angiotension sysmtem (RAS). It is essential in facilitating the conversion of angiotension to angiotension II, which is the active component of the system.<ref name="review">DOI: 10.1146/annurev.ph.40.030178.002113</ref> This system is responsible for the regulation of blood pressure, stimulation of the secretion of aldosterone which effects the salt and water balance.<ref name="review"/>
+[[Image:Man pic.png|thumb|left|Renin-Angiotensin-Aldosterone System]]
+Renin plays a key role in the Renin-Angiotension sysmtem (RAS). It is essential in facilitating the conversion of angiotension to angiotension II, which is the active component of the RAS system.<ref name="review">DOI: 10.1146/annurev.ph.40.030178.002113</ref> This system is responsible for the regulation of blood pressure, stimulation of the secretion of aldosterone which effects the salt and water balance.<ref name="review"/>
+*Angiotensinogen is released into the bloodstream by the liver.
+*Likewise, Renin is secreted by the kidneys into the bloodstream where is meets with angiotensinogen.
+*Once united, angiotensinogen form the decapeptide angiotensin (ANG) I.
+*ANG I is then activated by Angiotensin converting enzyme (ACE) to form the  octapeptide ANG II.
+*ANG II then acts on specific receptors such as ones responsible for vasoconstriction or the release of aldosterone from the adrenal cortex. <ref name="renin review"> doi: 10.1152/physrev.00036.2005
+</ref>