Flexible regions within the membrane-embedded portions of polytopic membrane proteins

Naotaka Hamasaki, Yoshito Abe, Michael J.A. Tanner

Research output: Contribution to journalShort survey

19 Citations (Scopus)

Abstract

The conventional view of the structure of the membrane-embedded regions of integral membrane proteins is that they are in contact with lipids that interact with the hydrophobic surfaces of the polypeptide, and therefore have intrinsically rigid α-helical structures. Here, we briefly review the evidence that in the case of integral membrane proteins with many membrane spans (including membrane transporters and channels), some membrane peptide segments are more or less completely shielded from the lipid bilayer by other membrane polypeptide portions. These portions do not need to have α-helical structures and are likely to be much more flexible than typical membrane-spanning helices. The ability of the band 3 anion exchanger to accommodate anionic substrates of different sizes, geometries, and charge distributions suggests the presence of flexible regions in the active center of this protein. These flexible substructures may have important functional roles in membrane proteins, particularly in the mechanisms of membrane transporters and channels.

Original languageEnglish
Pages (from-to)3852-3854
Number of pages3
JournalBiochemistry
Volume41
Issue number12
DOIs
Publication statusPublished - Mar 26 2002

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Membrane Proteins
Membranes
Membrane Transport Proteins
Ion Channels
Peptides
Chloride-Bicarbonate Antiporters
Lipid bilayers
Charge distribution
Lipid Bilayers
Lipids
Geometry
Substrates
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Flexible regions within the membrane-embedded portions of polytopic membrane proteins. / Hamasaki, Naotaka; Abe, Yoshito; Tanner, Michael J.A.

In: Biochemistry, Vol. 41, No. 12, 26.03.2002, p. 3852-3854.

Research output: Contribution to journalShort survey

Hamasaki, Naotaka ; Abe, Yoshito ; Tanner, Michael J.A. / Flexible regions within the membrane-embedded portions of polytopic membrane proteins. In: Biochemistry. 2002 ; Vol. 41, No. 12. pp. 3852-3854.
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