Sandbox Reserved 347
From Proteopedia
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==Biochemistry== | ==Biochemistry== | ||
| - | Renin is an aspartyl protease. <ref name= "Structure"> 2666611</ref> | + | Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref> |
==Function== | ==Function== | ||
Revision as of 23:37, 3 March 2011
| This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
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Contents |
Introduction
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| 2iko, resolution 1.90Å () | |||||||||
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| Ligands: | |||||||||
| Gene: | REN (Homo sapiens) | ||||||||
| Activity: | Renin, with EC number 3.4.23.15 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
- 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.
- Thus, it regulates the body's mean arterial blood pressure. [1]
Biochemistry
Renin is an aspartyl protease. [2]
Function
Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.
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