A structural model of human erythrocyte band 2.1

Alignment of chemical and functional domains

R. Wallin, E. N. Culp, D. B. Coleman, Steven Goodman

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Protein 2.1 is a 210-kilodalton protein that connects erythrocyte spectrin to the NH2-terminal cytoplasmic domain of band 3 and thereby functions as the essential linkage between the membrane skeleton and the bilayer. We cleaved this protein into specific chemical domains by limited digestion with trypsin and α-chymotrypsin at 0°C. Intermediate-sized peptides were separated by two-dimensional isoelectric focusing/NaDodSO4/polyacrylamide gel electrophoresis and characterized by high resolution peptide mapping. We have established a provisional structural model of protein 2.1 by comparing the peptide maps of these chemical domains to maps obtained from larger overlapping chymotrypsin fragments as well as fragments obtained from 2-nitro-5-thiocyanobenzoic acid cleavage. In addition to providing a provisional structural map of protein 2.1, we have identified two functional domains of protein 2.1, an 83-kilodalton tryptic peptide (T-83) which binds band 3 and a 65-kilodalton tryptic peptide (T-65) which binds spectrin. We have therefore localized the functional domains along our linear map of protein 2.1.

Original languageEnglish (US)
Pages (from-to)4095-4099
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume81
Issue number13 I
DOIs
StatePublished - Jan 1 1984

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Structural Models
Erythrocytes
Peptide T
Spectrin
Proteins
Peptides
Peptide Mapping
Chymotrypsin
Isoelectric Focusing
Skeleton
Polyacrylamide Gel Electrophoresis
Digestion
Membranes

All Science Journal Classification (ASJC) codes

  • General

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A structural model of human erythrocyte band 2.1 : Alignment of chemical and functional domains. / Wallin, R.; Culp, E. N.; Coleman, D. B.; Goodman, Steven.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 81, No. 13 I, 01.01.1984, p. 4095-4099.

Research output: Contribution to journalArticle

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N2 - Protein 2.1 is a 210-kilodalton protein that connects erythrocyte spectrin to the NH2-terminal cytoplasmic domain of band 3 and thereby functions as the essential linkage between the membrane skeleton and the bilayer. We cleaved this protein into specific chemical domains by limited digestion with trypsin and α-chymotrypsin at 0°C. Intermediate-sized peptides were separated by two-dimensional isoelectric focusing/NaDodSO4/polyacrylamide gel electrophoresis and characterized by high resolution peptide mapping. We have established a provisional structural model of protein 2.1 by comparing the peptide maps of these chemical domains to maps obtained from larger overlapping chymotrypsin fragments as well as fragments obtained from 2-nitro-5-thiocyanobenzoic acid cleavage. In addition to providing a provisional structural map of protein 2.1, we have identified two functional domains of protein 2.1, an 83-kilodalton tryptic peptide (T-83) which binds band 3 and a 65-kilodalton tryptic peptide (T-65) which binds spectrin. We have therefore localized the functional domains along our linear map of protein 2.1.

AB - Protein 2.1 is a 210-kilodalton protein that connects erythrocyte spectrin to the NH2-terminal cytoplasmic domain of band 3 and thereby functions as the essential linkage between the membrane skeleton and the bilayer. We cleaved this protein into specific chemical domains by limited digestion with trypsin and α-chymotrypsin at 0°C. Intermediate-sized peptides were separated by two-dimensional isoelectric focusing/NaDodSO4/polyacrylamide gel electrophoresis and characterized by high resolution peptide mapping. We have established a provisional structural model of protein 2.1 by comparing the peptide maps of these chemical domains to maps obtained from larger overlapping chymotrypsin fragments as well as fragments obtained from 2-nitro-5-thiocyanobenzoic acid cleavage. In addition to providing a provisional structural map of protein 2.1, we have identified two functional domains of protein 2.1, an 83-kilodalton tryptic peptide (T-83) which binds band 3 and a 65-kilodalton tryptic peptide (T-65) which binds spectrin. We have therefore localized the functional domains along our linear map of protein 2.1.

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