Abstract
A number of unusual seven-transmembrane molecules have recently been characterized that have significant amino acid sequence similarity within the membrane-spanning hydrophobic regions and intervening loops to members of G-protein-coupled receptor family B. However, in contrast to the family-B G-protein-coupled receptors, these molecules have unusually large N-terminal extracellular domains that contain a number of well- characterized protein modules. The range of cell types expressing these complex molecules and their potential roles in cell adhesion and signalling have become a major focus of research in a number of biological systems. Copyright (C) 2000 Elsevier Science Ltd.
| Original language | English |
|---|---|
| Pages (from-to) | 284-289 |
| Number of pages | 6 |
| Journal | Trends in Biochemical Sciences |
| Volume | 25 |
| Issue number | 6 |
| DOIs | |
| State | Published - 01 06 2000 |
| Externally published | Yes |
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