Slow, Reversible, Coupled Folding and Binding of the Spectrin Tetramerization Domain
نویسندگان
چکیده
منابع مشابه
Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex.
As the principal component of the membrane skeleton, spectrin confers integrity and flexibility to red cell membranes. Although this network involves many interactions, the most common hemolytic anemia mutations that disrupt erythrocyte morphology affect the spectrin tetramerization domains. Although much is known clinically about the resulting conditions (hereditary elliptocytosis and pyropoik...
متن کاملMolecular Studies of the Erythrocyte Spectrin Tetramerization Region.
Human erythrocyte spectrin dimers associate at the N-terminal region of α spectrin (αN) and the C-terminal region of β spectrin (βC) to form tetramers. We have prepared model peptides to study the tetramerization region. Based on phasing information obtained from enzyme digests, we prepared spectrin fragments consisting of the first 156 amino-acid residues and the first 368 amino-acid residues ...
متن کاملInteractions of the a-Spectrin N-terminal Region with b-Spectrin IMPLICATIONS FOR THE SPECTRIN TETRAMERIZATION REACTION*
Spectrin of the erythrocyte membrane skeleton is composed of aand b-spectrin, which associate to form heterodimers and tetramers. It has been suggested that a fractional domain (helix C) in the amino-terminal region of a-spectrin (Na region) bundles with another fractional domain in the carboxyl-terminal region of b-spectrin (Cb region) to yield a triple a-helical bundle and that this helical b...
متن کاملInteractions of the alpha-spectrin N-terminal region with beta-spectrin. Implications for the spectrin tetramerization reaction.
Spectrin of the erythrocyte membrane skeleton is composed of alpha- and beta-spectrin, which associate to form heterodimers and tetramers. It has been suggested that a fractional domain (helix C) in the amino-terminal region of alpha-spectrin (Nalpha region) bundles with another fractional domain in the carboxyl-terminal region of beta-spectrin (Cbeta region) to yield a triple alpha-helical bun...
متن کاملThe carboxyterminal EF domain of erythroid alpha-spectrin is necessary for optimal spectrin-actin binding.
Spectrin and protein 4.1R crosslink F-actin, forming the membrane skeleton. Actin and 4.1R bind to one end of β-spectrin. The adjacent end of α-spectrin, called the EF domain, is calmodulin-like, with calcium-dependent and calcium-independent EF hands. The severely anemic sph(1J)/sph(1J) mouse has very fragile red cells and lacks the last 13 amino acids in the EF domain, implying that the domai...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2012
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2012.10.012