Thrombospondin

From Proteopedia

spinqualitylabelsall models Human TSP-1 Nterminal complex with Arixtra heparin (PDB code 1za4) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Disease 4 Structural highlights Function Thrombospondin (TSP) are glycoproteins released in response to thrombin stimulation. TSP is a transient component of extracellular matrix in developing tissues[1]. Relevance TSP-1 and TSP-2 are potent inhibitors of angiogenesis and thus are studied in cancer treatments[2]. Disease TSP-2 mutation is associated with coronary artery disease[3]. Structural highlights The N-terminal of TSP-1 mediates its interaction with integrins during cell adhesion, with lipoproteinreceptor-related protein during uptake and clearance and with fibrinogen during platelet aggregation. The [4].

3D structures of thrombospondin

Updated on 19-August-2024

References

1. ↑ Adams JC. Thrombospondin-1. Int J Biochem Cell Biol. 1997 Jun;29(6):861-5. PMID:9304800
2. ↑ Lawler PR, Lawler J. Molecular basis for the regulation of angiogenesis by thrombospondin-1 and -2. Cold Spring Harb Perspect Med. 2012 May;2(5):a006627. doi:, 10.1101/cshperspect.a006627. PMID:22553494 doi:http://dx.doi.org/10.1101/cshperspect.a006627
3. ↑ Carlson CB, Liu Y, Keck JL, Mosher DF. Influences of the N700S thrombospondin-1 polymorphism on protein structure and stability. J Biol Chem. 2008 Jul 18;283(29):20069-76. Epub 2008 May 22. PMID:18499674 doi:10.1074/jbc.M800223200
4. ↑ Tan K, Duquette M, Liu JH, Zhang R, Joachimiak A, Wang JH, Lawler J. The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin. Structure. 2006 Jan;14(1):33-42. PMID:16407063 doi:10.1016/j.str.2005.09.017