Figure 3: LTBP1 N-terminus multimerizes in a head-to-head manner. | Scientific Reports

Figure 3: LTBP1 N-terminus multimerizes in a head-to-head manner.

From: Independent multimerization of Latent TGFβ Binding Protein-1 stabilized by cross-linking and enhanced by heparan sulfate

Figure 3: LTBP1 N-terminus multimerizes in a head-to-head manner.

(A) SEC-MALS analysis of NT2 in 2 mM calcium or 2 mM EGTA on a Superose 6 column. Spontaneous oligomerization in the presence of calcium resulted in a mix of monomer (M = 54 kDa), dimer (D = 124 kDa) and higher order structures (H = 565 kDa) (gray trace) whereas in 2 mM EGTA only a monomer was observed (orange). To verify that the dominant species was a dimer, this fraction was run again (blue) and had Mwt of 135 kDa (Rh = 7.6 nm ± 1.017%). (B) SAXS data was collected on a dimer of the NT1 region and analyzed by ab initio modelling. A panel of four representative ab initio models is shown. (C) The NT1 monomer can be modelled into the dimer envelope suggesting an end-to-end arrangement.

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