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Sökning: id:"swepub:oai:lup.lub.lu.se:4b900ad1-36df-4fc5-885b-d04adabafab6" > Effect of Phosphory...

  • Lenton, SamuelKeele University,University of Leeds,Institut Laue Langevin (författare)

Effect of Phosphorylation on a Human-like Osteopontin Peptide

  • Artikel/kapitelEngelska2017

Förlag, utgivningsår, omfång ...

  • Elsevier BV,2017
  • 11 s.

Nummerbeteckningar

  • LIBRIS-ID:oai:lup.lub.lu.se:4b900ad1-36df-4fc5-885b-d04adabafab6
  • https://lup.lub.lu.se/record/4b900ad1-36df-4fc5-885b-d04adabafab6URI
  • https://doi.org/10.1016/j.bpj.2017.03.005DOI

Kompletterande språkuppgifter

  • Språk:engelska
  • Sammanfattning på:engelska

Ingår i deldatabas

Klassifikation

  • Ämneskategori:art swepub-publicationtype
  • Ämneskategori:ref swepub-contenttype

Anmärkningar

  • The last decade established that the dynamic properties of the phosphoproteome are central to function and its modulation. The temporal dimension of phosphorylation effects remains nonetheless poorly understood, particularly for intrinsically disordered proteins. Osteopontin, selected for this study due to its key role in biomineralization, is expressed in many species and tissues to play a range of distinct roles. A notable property of highly phosphorylated isoforms of osteopontin is their ability to sequester nanoclusters of calcium phosphate to form a core-shell structure, in a fluid that is supersaturated but stable. In Biology, this process enables soft and hard tissues to coexist in the same organism with relative ease. Here, we extend our understanding of the effect of phosphorylation on a disordered protein, the recombinant human-like osteopontin rOPN. The solution structures of the phosphorylated and unphosphorylated rOPN were investigated by small-angle x-ray scattering and no significant changes were detected on the radius of gyration or maximum interatomic distance. The picosecond-to-nanosecond dynamics of the hydrated powders of the two rOPN forms were further compared by elastic and quasi-elastic incoherent neutron scattering. Phosphorylation was found to block some nanosecond side-chain motions while increasing the flexibility of other side chains on the faster timescale. Phosphorylation can thus selectively change the dynamic behavior of even a highly disordered protein such as osteopontin. Through such an effect on rOPN, phosphorylation can direct allosteric mechanisms, interactions with substrates, cofactors and, in this case, amorphous or crystalline biominerals.

Ämnesord och genrebeteckningar

Biuppslag (personer, institutioner, konferenser, titlar ...)

  • Grimaldo, MarcoUniversity of Tübingen,Institut Laue Langevin (författare)
  • Roosen-Runge, FelixLund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Institut Laue Langevin(Swepub:lu)fe2820ro (författare)
  • Schreiber, FrankUniversity of Tübingen (författare)
  • Nylander, TommyLund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)fk1-tny (författare)
  • Clegg, RogerHannah Research Institute (författare)
  • Holt, CarlUniversity of Glasgow (författare)
  • Härtlein, MichaelInstitut Laue Langevin (författare)
  • García Sakai, VictoriaRutherford Appleton Laboratory (författare)
  • Seydel, TiloInstitut Laue Langevin (författare)
  • Marujo Teixeira, Susana C.National Institute of Standards and Technology (NIST),University of Delaware (författare)
  • Keele UniversityUniversity of Leeds (creator_code:org_t)

Sammanhörande titlar

  • Ingår i:Biophysical Journal: Elsevier BV112:8, s. 1586-15960006-3495

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