Structural studies reveal an important role for the pleiotrophin C-terminus in mediating interactions with chondroitin sulfate.

ABSTRACT:

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Pleiotrophin (PTN) is a potent glycosaminoglycan-binding cytokine that is important in neural development, angiogenesis and tissue regeneration. Much of its activity is attributed to its interactions with the chondroitin sulfate (CS) proteoglycan, receptor type protein tyrosine phosphatase ζ (PTPRZ). However, there is little high resolution structural information on the interactions between PTN and CS, nor is it clear why the C-terminal tail of PTN is necessary for signaling through PTPRZ, even though it does not contribute to heparin binding. We determined the first structure of PTN and analyzed its interactions with CS. Our structure shows that PTN possesses large basic surfaces on both of its structured domains and also that residues in the hinge segment connecting th

SUBMITTER: Ryan E 

PROVIDER: S-EPMC6217956 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature