Abstract：
:The amino acid sequences of chick and slime mould alpha-actinin each contain four repeats of approximately 122 residues. These repeats are homologous to the 18-22 repeats, each of approximately 106 residues, found in the alpha and beta subunits of spectrin and fodrin, and to the multiple repeats of approximately 110 residues found in the Duchenne muscular dystrophy protein (dystrophin). The repeats correspond to the elongated rod-like portion of these molecules. We present a multiple sequence alignment of 21 repeats from this superfamily (8 alpha-actinin and 13 spectrin/fodrin), based on optimal pairwise alignments, from which a characteristic consensus pattern of amino acid types is deduced. Trp 46 is invariant in all but one repeat, and physicochemical classes of amino acids are conserved at 25 other positions. Secondary structure prediction on both the alpha-actinin and spectrin repeats taken together with the distribution of proline residues in the sequences, strongly suggest that each repeated domain consists of a four-helix structure. Our predictions differ significantly from previous three-helix models based on analyses of fewer sequences. To determine possible interdomain regions, sites of limited proteolysis of the native chick alpha-actinin dimer were determined and located in the amino acid sequence. The majority of these sites were in corresponding positions in different repeats within a segment predicted as a long helix. We propose a model, consistent with the overall dimensions of the rod-like portions of the molecules, in which these long, probably interrupted helices, link adjacent domains.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Davison MD,Baron MD,Critchley DR,Wootton JCdoi
10.1016/0141-8130(89)90047-0subject
Has Abstractpub_date
1989-04-01 00:00:00pages
81-90issue
2eissn
0141-8130issn
1879-0003pii
0141-8130(89)90047-0journal_volume
11pub_type
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journal_title：International journal of biological macromolecules
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journal_title：International journal of biological macromolecules
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journal_title：International journal of biological macromolecules
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journal_title：International journal of biological macromolecules
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journal_title：International journal of biological macromolecules
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journal_title：International journal of biological macromolecules
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journal_title：International journal of biological macromolecules
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journal_title：International journal of biological macromolecules
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