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Título: | Structure of a fragment of the integrin ß4 by hybrid methods: x-ray crystallography, small angle x-ray scattering and electron paramagnetic resonance spectroscopy |
Autor: | Pereda, José M. de CSIC ORCID | Fecha de publicación: | 2013 | Citación: | 11th International Conference on Biology and Synchrotron Radiation (2013) | Resumen: | The integrin α6ß4 is a component of the hemidesmosomes, protein complexes that mediate the stable anchoring of basal epithelial cells to the basement membrane. The cytodomain of ß4 is unique among the integrin family and it is responsible for the intracellular interactions of α6ß4. The cytoplasmic region of ß4 contains four fibronectin type III domains (FnIII) arranged in two pairs (FnIII-1,2 and FnIII-3,4) separated by a connecting segment (CS). A 90-residue C-terminal tail (C-tail) extends downstream the FnIII4. The CS and the C-tail are in close proximity in living keratinocytes, yet the structure of the FnIII-3,4 region was unknown. We have combined x-ray crystallography, small angle x-ray scattering (SAXS), site directed spin labelling (SDSL), and electron paramagnetic resonance spectroscopy (EPR) to elucidate the structure of the FnIII-3,4 region of ß4. The individual crystal structures of the FnIII-3 and the FnIII-4 were solved and refined against data to 1.6 Å and 1.8 Å resolution, respectively. SAXS analysis of the FnIII-3,4 suggested that, in spite of being connected by a 23-residue linker, these two FnIIIs adopt a compact structure. Modelling of the low resolution structure of the FnIII-3,4 using the SAXS data and ab initio methods revealed a heart-shaped compact structure. It was not possible to unambiguously dock the crystal structures of the FnIII-3 and the FnIII-4 into the SAXS-derived envelope, or to locate them by multi-domain rigid-body fitting against the SAXS data. Thus, we have combined SDSL and EPR to obtain inter-domain distances that served as restraints to elucidate the relative orientation of the FnIII3 and FnIII4. Our results have implications for the organization of the cytodomain of the integrin ß4 subunit and support an intramolecular interaction between the CS and the C-tail. | Descripción: | Resumen del trabajo presentado al 11th International Conference on Biology and Synchrotron Radiation (BSR), celebrado en Hamburgo (Alemania) del 8 al 11 de septiembre de 2013. | URI: | http://hdl.handle.net/10261/136094 |
Aparece en las colecciones: | (IBMCC) Comunicaciones congresos |
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