The face of TSR revealed: an extracellular signaling domain is exposed. J Cell Biol 2002 Oct 28;159(2):203-6
Date
10/31/2002Pubmed ID
12403807Pubmed Central ID
PMC2173053DOI
10.1083/jcb.200209138Scopus ID
2-s2.0-0037191044 (requires institutional sign-in at Scopus site) 30 CitationsAbstract
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.
Author List
Silverstein RLAuthor
Roy L. Silverstein MD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsExtracellular Space
Protein Structure, Tertiary
Signal Transduction
Thrombospondin 1