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Sandbox Reserved 347

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Revision as of 08:33, 4 April 2011 by Rhiannon Khela (Talk | contribs)
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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.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing


PDB ID 2iko

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2iko, resolution 1.90Å ()
Ligands:
Gene: REN (Homo sapiens)
Activity: Renin, with EC number 3.4.23.15
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

Introduction

(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. [1]


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. [2] 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. [1] Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.[3]

Biochemistry

Renin-Angiotensin-Aldosterone System
Renin-Angiotensin-Aldosterone System

Renin is an aspartyl protease. [4]

Renin active site

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  • 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.[5] This system is responsible for the regulation of blood pressure, stimulation of the secretion of aldosterone which effects the salt and water balance.[5]


Ligand site

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References

  1. ↑ 1.0 1.1 Gradman AH, Kad R. Renin inhibition in hypertension. J Am Coll Cardiol. 2008 Feb 5;51(5):519-28. PMID:18237679 doi:10.1016/j.jacc.2007.10.027
  2. ↑ 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
  3. ↑ Armstrong C. The vision of the pore. Science. 1998 Apr 3;280(5360):56-7. PMID:9556453
  4. ↑ Inagami T. Structure and function of renin. J Hypertens Suppl. 1989 Apr;7(2):S3-8. PMID:2666611
  5. ↑ 5.0 5.1 Reid IA, Morris BJ, Ganong WF. The renin-angiotensin system. Annu Rev Physiol. 1978;40:377-410. PMID:205167 doi:http://dx.doi.org/10.1146/annurev.ph.40.030178.002113
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