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

Pub. Date : 2016 Apr

PMID : 26896299






15 Functional Relationships(s)
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1 Structural studies reveal an important role for the pleiotrophin C-terminus in mediating interactions with chondroitin sulfate. Chondroitin Sulfates pleiotrophin Homo sapiens
2 We determined the first structure of PTN and analyzed its interactions with CS. Chondroitin Sulfates pleiotrophin Homo sapiens
3 Our analysis of PTN-CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ. Chondroitin Sulfates pleiotrophin Homo sapiens
4 Our analysis of PTN-CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ. Chondroitin Sulfates pleiotrophin Homo sapiens
5 Our analysis of PTN-CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ. Chondroitin Sulfates pleiotrophin Homo sapiens
6 Our analysis of PTN-CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ. Chondroitin Sulfates pleiotrophin Homo sapiens
7 NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. Chondroitin Sulfates pleiotrophin Homo sapiens
8 NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. Chondroitin Sulfates pleiotrophin Homo sapiens
9 NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. Chondroitin Sulfates pleiotrophin Homo sapiens
10 NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. Chondroitin Sulfates pleiotrophin Homo sapiens
11 NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. Chondroitin Sulfates pleiotrophin Homo sapiens
12 NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. Chondroitin Sulfates pleiotrophin Homo sapiens
13 NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. Chondroitin Sulfates pleiotrophin Homo sapiens
14 NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. Chondroitin Sulfates pleiotrophin Homo sapiens
15 NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. Chondroitin Sulfates pleiotrophin Homo sapiens