1LSL
Crystal Structure of the Thrombospondin-1 Type 1 Repeats
Summary for 1LSL
| Entry DOI | 10.2210/pdb1lsl/pdb |
| Descriptor | Thrombospondin 1, beta-L-fucopyranose, alpha-L-fucopyranose, ... (4 entities in total) |
| Functional Keywords | tsp-1, tsr, cell adhesion |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 12504.94 |
| Authors | Tan, K.,Duquette, M.,Liu, J.,Dong, Y.,Zhang, R.,Joachimiak, A.,Lawler, J.,Wang, J.-H. (deposition date: 2002-05-17, release date: 2002-12-18, Last modification date: 2024-10-30) |
| Primary citation | Tan, K.,Duquette, M.,Liu, J.H.,Dong, Y.,Zhang, R.,Joachimiak, A.,Lawler, J.,Wang, J.H. Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication. J.Cell Biol., 159:373-382, 2002 Cited by PubMed Abstract: Thrombospondin-1 (TSP-1) contains three type 1 repeats (TSRs), which mediate cell attachment, glycosaminoglycan binding, inhibition of angiogenesis, activation of TGFbeta, and inhibition of matrix metalloproteinases. The crystal structure of the TSRs reported in this article reveals a novel, antiparallel, three-stranded fold that consists of alternating stacked layers of tryptophan and arginine residues from respective strands, capped by disulfide bonds on each end. The front face of the TSR contains a right-handed spiral, positively charged groove that might be the "recognition" face, mediating interactions with various ligands. This is the first high-resolution crystal structure of a TSR domain that provides a prototypic architecture for structural and functional exploration of the diverse members of the TSR superfamily. PubMed: 12391027DOI: 10.1083/jcb.200206062 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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