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Peptide‐specific antibodies localize the major lipid binding sites of talin dimers to oppositely arranged N‐terminal 47 kDa subdomains 1
Author(s) -
Isenberg Gerhard,
Goldmann Wolfgang H.
Publication year - 1998
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/s0014-5793(98)00336-6
Subject(s) - antiparallel (mathematics) , polyclonal antibodies , dimer , chemistry , peptide , peptide sequence , amino acid , biochemistry , binding domain , binding site , biophysics , stereochemistry , antibody , biology , physics , organic chemistry , quantum mechanics , magnetic field , gene , immunology
Using ultrastructural analysis and labeling with polyclonal antibodies that recognize peptide sequences specific for phospholipid binding, we mapped the functional domain structure of intact platelet talin and its proteolytic fragments. The talin dimer, which is crucial for actin and lipid binding, is built of a backbone containing the 200 kDa rod portions, at both ends of which a 47 kDa globular domain is attached. Peptide‐specific polyclonal antibodies were raised against three potential lipid binding sequences residing within the N‐terminal 47 kDa domain (i.e. S19, amino acids 21–39; H18, amino acids 287–304; and H17, amino acids 385–406). Antibodies H17 and H18 localize these lipid binding sequences within the N‐terminal 47 kDa globular talin subdomains opposed at the outer 200 kDa rod domains within talin dimers. Hence, we conclude that in its dimeric form, which is used in actin and lipid binding, talin is a dumbbell‐shaped molecule built of two antiparallel subunits.