Murine and human T11 (CD2) cDNA sequences suggest a common signal transduction mechanism.
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 beta sheets, we predict that mouse and human T11 external domains probably belong to the alpha/beta protein folding class. The cytoplasmic region of T11 is a lengthy, proline-rich segment; 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.
Clayton
L K
LK
Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston, MA 02115.
Sayre
P H
PH
Novotny
J
J
Reinherz
E L
EL
D000595:Amino Acid Sequence; D000818:Animals; D000954:Antigens, Surface / Q000235:genetics* / Q000502:physiology; D001483:Base Sequence; D004247:DNA / Q000235:genetics; D005796:Genes; D006801:Humans; D051379:Mice / Q000235:genetics*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D018127:Tumor Necrosis Factor Receptor Superfamily, Member 7
D000954:Antigens, Surface; D018127:Tumor Necrosis Factor Receptor Superfamily, Member 7; D004247:DNA