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.

More help: Help:Editing

Introduction

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2iko, resolution 1.90Å (default scene)
Ligands: 7IG
Gene: REN (Homo sapiens)
Activity: Renin, with EC number 3.4.23.15
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Renin (pronounced /ˈriːnɨn/ REE-nin)is also known as angiotensinogenase,an enzyme that participates in the body's renin-angiotensin system (RAS) which mediates extracellular volume and arterial vasoconstriction.
Thus, it regulates the body's mean arterial blood pressure. [1]

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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. ↑ Akahane K, Umeyama H, Nakagawa S, Moriguchi I, Hirose S, Iizuka K, Murakami K. Three-dimensional structure of human renin. Hypertension. 1985 Jan-Feb;7(1):3-12. PMID:3884499
  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