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Integral membrane protein



An Integral Membrane Protein (IMP) is a protein molecule (or assembly of proteins) that is permanently attached to the biological membrane. Such proteins can be separated from the biological membranes only using detergents, nonpolar solvents, or sometimes denaturing agents.

IMPs comprise a very significant fraction of the proteins encoded in the genome.

Additional recommended knowledge

Contents

Structure

3D structures of only ~160 different integral membrane proteins are currently determined at atomic resolution by X-ray crystallography or Nuclear magnetic resonance spectroscopy due to the difficulties with extraction and crystallization. In addition, structures of many water-soluble domains of IMPs are available in the Protein Data Bank. Their membrane-anchoring α-helices have been removed to facilitate the extraction and crystallization.

IMPs can be divided into two groups:

  1. Transmembrane proteins
  2. Integral monotopic proteins

Integral transmembrane protein

Transmembrane proteins span the entire biological membrane. This is the most common type of IMP.

Integral monotopic proteins

Integral monotopic proteins are permanently attached to the membrane from one side.

Three-dimensional structures of the following integral monotopic proteins have been determined:

  • prostaglandin H2 syntheses 1 and 2 (cyclooxygenases) [1],
  • lanosterol synthase and squalene-hopene cyclase [2],
  • microsomal prostaglandin E synthase [3],
  • carnitine O-palmitoyltransferase 2 [4].

There are also structures of integral monotopic domains of transmembrane proteins:

Such domains require detergents for extraction or crystallization, even after removal of their transmembrane helices. Therefore, they are often classified as integral monotopic proteins [9]

Function

IMPs include transporters, channels, receptors, enzymes, structural membrane-anchoring domains, proteins involved in accumulation and transduction of energy, and proteins responsible for cell adhesion. Classification of transporters can be found in TCDB database.

References

  • Booth, P.J., Templer, R.H., Meijberg, W., Allen, S.J., Curran, A.R., and Lorch, M. 2001. In vitro studies of membrane protein folding. Crit. Rev. Biochem. Mol. Biol. 36: 501-603.
  • Bracey M.H., Cravatt B.F., Stevens R.C., Cravatt B.F. 2004. Structural commonalities among integral membrane enzymes. FEBS Lett. 567: 159-165.
  • Bowie J.U. 2001. Stabilizing membrane proteins. Curr. Op. Struct. Biol. 11: 397-402.
  • Bowie J.U. 2005. Solving the membrane protein folding problem. Nature 438: 581-589.
  • DeGrado W.F., Gratkowski H. and Lear J.D. 2003. How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles. Protein Sci. 12: 647-665.
  • Popot J-L. and Engelman D.M. 2000. Helical membrane protein folding, stability, and evolution. Annu. Rev. Biochem. 69: 881-922.
  • Protein-lipid interactions (Ed. L.K. Tamm) Wiley, 2005.

See also

Examples

Examples of integral membrane proteins:

 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Integral_membrane_protein". A list of authors is available in Wikipedia.
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