Volume 17, Issue 9 pp. 1367-1370
Article
Full Access

Murine and human T11 (CD2) cDNA sequences suggest a common signal transduction mechanism

Linda K. Clayton

Corresponding Author

Linda K. Clayton

Department of Pathology, Harvard Medical School, Boston

Laboratory of Immunobiology, Dana-Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, USASearch for more papers by this author
Peter H. Sayre

Peter H. Sayre

Laboratory of Cellular and Molecular Research, Massachusetts General Hospital, Boston

Search for more papers by this author
Jiri Novotny

Jiri Novotny

Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston

Search for more papers by this author
Ellis L. Reinherz

Ellis L. Reinherz

Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston

Department of Medicine, Harvard Medical School, Boston

Search for more papers by this author
First published: 1987
Citations: 33

Abstract

The murine equivalent of the cDNA encoding the human T11 (CD2) sheep erythrocyte-binding protein has been cloned. It codes for a putative transmembrane protein which is homologous to human T11. In contrast to immunoglobulins whose domains consist of anti-parallel β sheets, we predict that mouse and human T11 external domains probably belong to the α/β protein folding class. The cytoplasmic region of T11 is a lengthy, proline-rich semgent; secondary structural analysis predicts it to have a nonglobular conformation. This elongated tail could allow for interaction with multiple other intracellular proteins and may contain a cation-binding site involved in T lineage activation.

The full text of this article hosted at iucr.org is unavailable due to technical difficulties.