Molecular Cloning of Ly-1, a Membrane Glycoprotein of Mouse T Lymphocytes and a Subset of B Cells: Molecular Homology to Its Human Counterpart Leu-1/T1 (CD5)

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1987 Jan 1

PMID 3025855

Citations 47

Authors

H J Huang

N H Jones

J L Strominger

L A Herzenberg

Affiliations

Soon will be listed here.

Abstract

We report the isolation of cDNA clones of the mouse lymphocyte differentiation antigen Ly-1. One of these cDNA clones was confirmed to be full-length by DNA sequencing and by expression of Ly-1 by L cells transfected with this clone. Analysis of the predicted amino acid sequence indicated that the Ly-1 polypeptide is synthesized with a 23 amino acid leader and that the mature protein consists of an amino-terminal region of 347 amino acids, a transmembrane sequence of 30 residues, and a carboxyl-terminal region of 94 amino acids. The amino-terminal region appears to be divided into two subregions by a threonine- and proline-rich sequence of 23 amino acids that is highly conserved between Ly-1 and its human homologue Leu-1 (CD5) in position and amino acid composition. The first amino-terminal subregion of 111 amino acids is predicted to be arranged in a beta-pleated sheet structure of six strands. The entire amino-terminal region is rich in cysteine, with all of its 22 cysteine residues conserved between Ly-1 and Leu-1. The carboxyl-terminal region has no cysteines. Ly-1 and Leu-1 are 63% identical, with a gradient of identical residues from 43% for the first amino-terminal subregion to 58% for the second amino-terminal subregion and 90% for the carboxyl-terminal region. The predicted secondary structure of the first amino-terminal subregion and identities of certain conserved residues among most members of the immunoglobulin gene superfamily suggest that Ly-1 and Leu-1 are distant members of this family.

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