The face of TSR revealed: an extracellular signaling domain is exposed.
In this issue, Tan et al. (2002) report the first high resolution (1.9 A) structural data for thrombospondin (TSP)-1, a large multifunctional protein that regulates cell adhesion, angiogenesis, cell proliferation and survival, TGFbeta activation, and protease function (for review see Chen et al., 2000). Because TSP-1 has multiple binding partners and many functions, precise structural information is crucial to understanding its biology. The structure now reported, derived from crystals of the second and third type I repeats of TSP-1 is of particular interest because of the specific functions attributed to these repeats and because domains homologous to the repeats appear in many other proteins in nature. The novel layered fold motif described brings great insight into how the complicated functions of TSP-1 and related molecules are affected.
Silverstein
Roy L
RL
Division of Hematology and Medical Oncology, Department of Medicine, Weill Medical College of Cornell University, New York, NY 10021, USA. rsilve@med.cornell.edu
D000818:Animals; D005110:Extracellular Space; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology*; D019700:Thrombospondin 1 / Q000737:chemistry* / Q000502:physiology*
D019700:Thrombospondin 1