Sandbox Reserved 313

Revision as of 07:32, 17 March 2011 by Justine Doherty (talk | contribs)
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 2dds

Drag the structure with the mouse to rotate
2dds, resolution 1.80Å ()
Ligands:
Activity: Sphingomyelin phosphodiesterase, with EC number 3.1.4.12
Related: 2ddr, 2ddt
Resources: FirstGlance, OCA, PDBsum, RCSB, TOPSAN
Coordinates: save as pdb, mmCIF, xml


IntroductionIntroduction

Sphingomyelin phosphodiesterase (SMase) is an enzyme which catalyzes the hydrolysis of sphingomyelin to ceramide and phosphocholine [1]. There are 6 known types of sphingomyelinases:

Acid sphingomyelinase (aSMase) -

Secretory sphingomyelinase (sSMase) -

Neutral, Mg2+-dependent sphingomyelinases (nSMase) -

Mg2+-independent neutral sphingomyelinases -

Alkaline sphingomyelinase -

Bacterial sphingomyelinase -

Structure and FunctionStructure and Function

MechanismMechanism

Importance of SMaseImportance of SMase

ReferencesReferences

  1. Ago H, Oda M, Takahashi M, Tsuge H, Ochi S, Katunuma N, Miyano M, Sakurai J. Structural basis of the sphingomyelin phosphodiesterase activity in neutral sphingomyelinase from Bacillus cereus. J Biol Chem. 2006 Jun 9;281(23):16157-67. Epub 2006 Apr 4. PMID:16595670 doi:10.1074/jbc.M601089200

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Justine Doherty