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Structure of the spectrin-actin binding site of erythrocyte protein 4.1.
The complete primary structure of the functional site of erythrocyte protein 4.1 involved in spectrin-actin associations has been determined. The sequence of this domain, which contains 67 amino acids and has a molecular mass of 8045 daltons, has been obtained by NH2-terminal sequence analysis of an 8-kDa chymotryptic peptide, three endoproteinase lysine C-cleaved peptides and two peptides obtained by Staphylococcus aureus protease V8 cleavage. All peptides including the 8-kDa domain peptide were purified by reverse-phase high performance liquid chromatography. Antibodies against two different synthetic peptides of the 8-kDa domain are able to inhibit the association between protein 4.1, spectrin, and F-actin, corroborating that the 8-kDa domain is responsible for the formation of a ternary complex. A computer search of the 8-kDa sequence with the National Biomedical Research Foundation database did not detect any significant homologies to known sequences. Protein 4.1 is not related to any known proteins and may represent a new protein superfamily.
PMID: 3531202 [PubMed - indexed for MEDLINE]
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Cited by 17 PubMed Central articles
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Protein 4.1R self-association: identification of the binding domain.
Pérez-Ferreiro CM, Lospitao E, Correas I.
Biochem J. 2006 Dec 15; 400(3):457-65.
[Biochem J. 2006]
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The N-terminal 209-aa domain of high molecular-weight 4.1R isoforms abrogates 4.1R targeting to the nucleus.
Luque CM, Lallena MJ, Pérez-Ferreiro CM, de Isidro Y, De Cárcer G, Alonso MA, Correas I.
Proc Natl Acad Sci U S A. 1999 Dec 21; 96(26):14925-30.
[Proc Natl Acad Sci U S A. 1999]
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Drosophila coracle, a member of the protein 4.1 superfamily, has essential structural functions in the septate junctions and developmental functions in embryonic and adult epithelial cells.
Lamb RS, Ward RE, Schweizer L, Fehon RG.
Mol Biol Cell. 1998 Dec; 9(12):3505-19.
[Mol Biol Cell. 1998]
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