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Fig. 5. Contributions of the RGD motif and L-lectin domain to ECM deposition. (A) Structural similarity of TSP1 C-terminal globular domain to L-type lectins. Left, TSP1 type3_5-7GCT crystal structure (PDB1ux6) (Kvansakul et al., 2004) with the type 3 repeats in yellow, the L-lectin domain in orange and calcium ions as blue spheres. The remaining type 3 repeats and two EGF domains in light grey were modelled from the homologous TSP2 structure (PDB1yo8) (Carlson et al., 2005). The RGD and DDD motifs in TSP1 (see text) are shown in atomic detail. The putative CD47-binding motifs (Gao et al., 1996) are in green. Right, crystal structure of VIP36 carbohydrate-recognition domain in complex with calcium (blue sphere) and a mannose trisaccharide (carbon and oxygen atoms shown in green and red, respectively) (PDB2e6v) (Satoh et al., 2007). The side chain of Asp131 (see text) is shown in atomic detail. (B,C) Cell attachment to wild-type or mutant TSP1 C-terminal monomer fragments. C2C12 and HASMC (B), or strain-matched wild-type or CD47-null mouse fibroblasts (C) were adhered to surfaces coated with 1 µM of each protein for 1 hour under serum-free conditions. Each column represents the mean from three experiments, bars=s.e.m. (D,E) Quantification of the relative expression (D) or ECM retention (E) of wild-type and mutant mRFPovTSP1C proteins. Each column represents the mean of three independent experiments; bars represent s.e.m. ^*P=0.02; ^**P=0.009.

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