Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin.

By L. Fisher, D. Torchia, B. Fohr, M. Young, N. Fedarko. Biochemical and Biophysical Research Communications - BBRC, 2001

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Bone sialoprotein (BSP) and osteopontin (OPN) are two members of the SIBLING (Small Integrin-Binding LIgand, N-linked Glycoprotein) family of genetically related proteins that are clustered on human chromosome 4. We present evidence that this entire family is the result of duplication and subsequent divergent evolution of a single ancient gene. The solution structures of these two post-translationally modified recombinant proteins were solved by one dimensional proton NMR and transverse relaxation times. The polypeptide backbones of both free BSP and OPN rapidly sample an ensemble of conformations consistent with them both being completely unstructured in solution. This flexibility appears to enable these relatively small glycoproteins to rapidly associate with a number of different binding partners including other proteins as well as the mineral phase of bones and teeth. These proteins often function by bridging two proteins of fixed structures into a biologically active complex.

Subfields: Materials Chemistry, Molecular Biology, Rheumatology

View Paper: https://www.semanticscholar.org/paper/f2eef944ccee13ebfcac18d6b8999df247b2ce39

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Citations in the corpus

Natively unfolded proteins: A point where biology waits for physics (2002, background): “…contacts (e.g., Abercrombie et al. 1978; Cary et al. 1980, 1981; Cho et al. 1996; Eom et al. 1996; Lisse et al. 1996; Penkett et al. 1997; Fletcher et al. 1998; Zhang and Matthews 1998; Bose et al. 1999; Uversky et al. 1999; Campbell et al. 2000; Fisher et al. 2001; DiGiammarino et al. 2001).”