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Binding sites involved in the interaction of actin with the N‐terminal region of dystrophin
Author(s) -
Levine B.A.,
Moir A.J.G.,
Patchell V.B.,
Perry S.V.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80019-d
Subject(s) - actin , binding site , dystrophin , peptide sequence , binding domain , amino acid residue , sequence (biology) , actin binding protein , chemistry , biochemistry , actina , amino acid , protein filament , biophysics , biology , actin cytoskeleton , cytoskeleton , gene , cell
Two actin‐binding sites have been identified on human dystrophin by proton NMR spectroscopy of synthetic peptides corresponding to defined regions of the polypeptide sequence. These are Actin‐Binding Site 1 (ABS1) located at residues 17–26 and Actin‐Binding Site 2 (ABS2) in the region of residues 128–156. Using defined fragments of the actin amino acid sequence, ABS1 has been shown to bind to actin in the region represented by residues 83–117 and ABS2 to the C‐terminal region represented by residues 350–375. These dystrophin‐binding sites lie on the exposed domain in the actin filament.