PRIMARY STRUCTURE OF LIGHT AND HEAVY-CHAIN VARIABLE REGIONS OF ANTIBODIES RECOGNIZING PHOSPHORYLATED VIMENTINS

Citation
S. Tsujino et al., PRIMARY STRUCTURE OF LIGHT AND HEAVY-CHAIN VARIABLE REGIONS OF ANTIBODIES RECOGNIZING PHOSPHORYLATED VIMENTINS, Biochemical and biophysical research communications, 219(2), 1996, pp. 633-637
Citations number
11
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006291X
Volume
219
Issue
2
Year of publication
1996
Pages
633 - 637
Database
ISI
SICI code
0006-291X(1996)219:2<633:PSOLAH>2.0.ZU;2-3
Abstract
We determined the primary structure of three types of monoclonal antib odies against phosphorylated vimentin, 4A4, YT33, and MO82, which reco gnize phosphorylated Ser55, Ser33, and Ser82 on vimentin, respectively . The amino acid sequences between these antibodies and the anti-phosp hotyrosine antibodies previously reported, (Asn/Gln)-X-(Gln/Tyr)-Ser-T yr in the complimentarity determining region (CDR) 3 of the light chai n of 4A4 and YT33, -(Ser/Thr)-(Ser/Thr)-Tyr-Asn-Gln-(Arg/Lys)-Phe-Lys in the heavy chain CDR2 of MO82, and Lys-X-Ser-(Ser/Asn) in the heavy chain CDR3 of YT33 and MO82, were highly conserved. These motifs may p lay a role in recognizing phosphate groups of phosphoserine and phosph otyrosine. (C) 1996 Academic Press, Inc.