Sandbox Reserved 347

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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.

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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 the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate. [2]

Biochemistry

Renin is an aspartyl protease. [3]

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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.

Ligand site

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References

  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. 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
  3. Inagami T. Structure and function of renin. J Hypertens Suppl. 1989 Apr;7(2):S3-8. PMID:2666611
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