Sandbox Reserved 347: Difference between revisions

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=intro=
 
{{STRUCTURE_2iko | PDB=2iko | SCENE= }}
{{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }}
:Renin (pronounced /ˈriːnɨn/ REE-nin), also known as angiotensinogenase is an enzyme that participates in the body's renin-angiotensin system (RAS) that mediates extracellular volume (i.e., that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction.  
=Introduction=
::Thus, it regulates the body's mean arterial blood pressure.
<scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II.  Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. <ref name="hypertension">doi:10.1016/j.jacc.2007.10.027
</ref>
 
 
==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> 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>   
 
 
 
<Structure load='2iko' size='500' frame='true' align='right' caption='Renin active site' scene='Sandbox_Reserved_347/Ligand/1' />
 
 
 
 
==Function==
[[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>
 
 
 
<Structure load='2iko' size='300' frame='true' align='left' caption='Renin: Displaying the Ligand site' scene='Insert optional scene name here' />
 
=References=
<references/>