The identification and structural analysis of potential 14‐3‐3 interaction sites on the bone regulator protein Schnurri‐3

14‐3‐3 proteins regulate many intracellular processes and their ability to bind in subtly different fashions to their numerous partner proteins provides attractive drug‐targeting points for a range of diseases. Schnurri‐3 is a suppressor of mouse bone formation and a candidate target for novel osteo...

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Vydáno v:	Acta crystallographica. Section F, Structural biology communications Ročník 77; číslo 8; s. 254 - 261
Hlavní autoři:	Soini, Lorenzo, Leysen, Seppe, Crabbe, Tom, Davis, Jeremy, Ottmann, Christian
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.08.2021 Wiley Subscription Services, Inc
Témata:	14-3-3 Proteins - chemistry 14-3-3 Proteins - genetics 14-3-3 Proteins - metabolism 14‐3‐3 modes Amino Acid Sequence Animals Binding Sites - physiology Biomedical materials Bone growth bone regulator protein Calorimetry Crystallography Crystallography, X-Ray - methods disulfide bonds DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Fluorescence Fluorescence polarization Humans Mice Osteogenesis Osteogenesis - physiology Osteoporosis Peptides phosphorylation Protein Structure, Secondary Protein Structure, Tertiary Proteins Research Communications Schnurri‐3 Structural analysis Synthetic peptides Therapeutic targets Titration Titration calorimetry X‐ray protein crystallography Zinc Fingers - physiology Schnurri-3 disulfide bonds bone regulator protein fluorescence polarization phosphorylation 14-3-3 modes X-ray protein crystallography
ISSN:	2053-230X, 2053-230X
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Shrnutí:	14‐3‐3 proteins regulate many intracellular processes and their ability to bind in subtly different fashions to their numerous partner proteins provides attractive drug‐targeting points for a range of diseases. Schnurri‐3 is a suppressor of mouse bone formation and a candidate target for novel osteoporosis therapeutics, and thus it is of interest to determine whether it interacts with 14‐3‐3. In this work, potential 14‐3‐3 interaction sites on mammalian Schnurri‐3 were identified by an in silico analysis of its protein sequence. Using fluorescence polarization, isothermal titration calorimetry and X‐ray crystallography, it is shown that synthetic peptides containing either phosphorylated Thr869 or Ser542 can indeed interact with 14‐3‐3, with the latter capable of forming an interprotein disulfide bond with 14‐3‐3σ: a hitherto unreported phenomenon. The structures of two peptide motifs of Schnurri‐3 in complex with 14‐3‐3 are reported.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	2053-230X 2053-230X
DOI:	10.1107/S2053230X21006658