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PMID: 2367532 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

On the structure of erythrocyte spectrin in partially expanded membrane skeletons.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 87 ·No. 13 ·1990-07-00 ·Pages 5208-12

McGough AM, Josephs R

Abstract

Spectrin is generally believed to play an important role in the erythrocyte membrane's ability to deform elastically. We have studied the structure of negatively stained spectrin in partially expanded membrane skeletons to determine how its molecular structure confers elastic properties on the cell membrane. Fourier analysis of electron micrographs of spectrin reveals that the alpha and beta subunits are twisted about a common axis, forming a two-start helix with twofold rotational symmetry. We propose that elastic deformation of the cell is mediated by transient extension of the helix by mechanical forces.

MeSH Terms
Computer Simulation Erythrocyte Membrane/ultrastructure Humans Macromolecular Substances Microscopy, Electron Models, Structural Protein Conformation Spectrin/ultrastructure
Chemicals
Macromolecular Substances Spectrin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
McGough A M
Department of Molecular Genetics and Cell Biology, University of Chicago, IL 60637.
Josephs R
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21 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.87.13.5208
Published
1990-07-00
Pages
5208-12
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC54291
Subset
IM
Grants
NIGMS NIH HHS · GM07183 · United States
NHLBI NIH HHS · HL22654 · United States
External Links
PubMed source DOI: 10.1073/pnas.87.13.5208 PMC Full Text View journal details
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