Fig. 3: BFPA cross-linkers identifies differential cross-links and interactions in importin complex. | Communications Biology

Fig. 3: BFPA cross-linkers identifies differential cross-links and interactions in importin complex.

From: Towards a universal cross-linking mass spectrometry approach for protein structure analysis with homo-bi-functional photo-activatable cross-linkers

Fig. 3

A–C Importin complex (KPNA2-KPNB1) cross-links by DSSO (blue, left), SDA (purple, center), EBDA (green, right) and BBDA (orange, right). Red: IBB domain. Purple: NLS binding domains. Yellow: HEAT repeat regions that are cross-linked. D–F Structure of importin alpha-1 IBB domain in pink interacting with importin beta in grey (PDB: 1QGK). DSSO, SDA EBDA/BBDA cross-links mapped to structure. G–I Structure of full-length importin alpha-1 in pink interacting with importin beta in grey predicted by Alphafold Multimer. J, K Plot of percentage of cross-links which satisfy 30 Å distance constraint or amino acid adjusted distance constraint respectively for 1QGK structure and AlphaFold predicted structures. pTM scores are listed below the rank of the AlphaFold model. L Amino acid frequency of cross-link sites for Importin complex cross-links from DSSO (blue), SDA (purple), EBDA (green) and BBDA (orange) cross-linkers.

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