Would be transient, allowing short-term access to a binding MedChemExpress 10236-47-2 surface that would then be stabilized. We note that 22948146 phosphorylation of ILK at Thr-173, within the unstructured linker of ILK, has been demonstrated [49], potentially presenting a mechanism by which the linker could stabilize inter-domain interaction in the cell. Alternatively, inter-domain 
contacts within IPP could provide a contiguous binding site for a binding partner when properly aligned. However, it does not appear that IPP is pre-SPI 1005 biological activity aligned for a binding event involving a contiguous surface, since we detect some flexibility in IPP. ILK reportedly interacts directly with integrin btails and kindlin [3,25], PINCH1 binds Nck-2 [50], and a-parvin binds paxillin and F-actin [16,51]. It will therefore be interesting to see whether these and other binding events are associated with distinct conformational states of the IPP complex.SAXS Analysis of the IPP ComplexSupporting InformationFigure S1 Automatic Guinier Analysis. Linear region of the Guinier plots as determined automatically by AutoRG (Primus) [29]. The Rg values are presented in Table S1. (TIFF) Table S1 Rg values determined by automatic Guinier Analysis in AutoRG [29]. (DOC)AcknowledgmentsWe thank Brian Chiswell, Rong Zhang, Hiro Tsuruta, and Tsutomu Matsui.Author ContributionsConceived and designed 
the experiments: ALS TJB. Performed the experiments: ALS TDG JRL EHS. Analyzed the data: ALS TDG EHS TJB. Contributed reagents/materials/analysis tools: ALS TDG JRL DAC EHS TJB. Wrote the paper: ALS TJB.Would be transient, allowing short-term access to a binding surface that would then be stabilized. We note that 22948146 phosphorylation of ILK at Thr-173, within the unstructured linker of ILK, has been demonstrated [49], potentially presenting a mechanism by which the linker could stabilize inter-domain interaction in the cell. Alternatively, inter-domain contacts within IPP could provide a contiguous binding site for a binding partner when properly aligned. However, it does not appear that IPP is pre-aligned for a binding event involving a contiguous surface, since we detect some flexibility in IPP. ILK reportedly interacts directly with integrin btails and kindlin [3,25], PINCH1 binds Nck-2 [50], and a-parvin binds paxillin and F-actin [16,51]. It will therefore be interesting to see whether these and other binding events are associated with distinct conformational states of the IPP complex.SAXS Analysis of the IPP ComplexSupporting InformationFigure S1 Automatic Guinier Analysis. Linear region of the Guinier plots as determined automatically by AutoRG (Primus) [29]. The Rg values are presented in Table S1. (TIFF) Table S1 Rg values determined by automatic Guinier Analysis in AutoRG [29]. (DOC)AcknowledgmentsWe thank Brian Chiswell, Rong Zhang, Hiro Tsuruta, and Tsutomu Matsui.Author ContributionsConceived and designed the experiments: ALS TJB. Performed the experiments: ALS TDG JRL EHS. Analyzed the data: ALS TDG EHS TJB. Contributed reagents/materials/analysis tools: ALS TDG JRL DAC EHS TJB. Wrote the paper: ALS TJB.
