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Receptor-Like Protein Tyrosine Phosphatase α Homodimerizes on the Cell Surface

We reported previously that the N-terminal D1 catalytic domain of receptor protein-tyrosine phosphatase α (RPTPα) forms a symmetrical, inhibited dimer in a crystal structure, in which a helix-turn-helix wedge element from one monomer is inserted into the catalytic cleft of the other monomer. Previou...

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Bibliografski detalji
Glavni autori: Jiang, Guoqiang, den Hertog, Jeroen, Hunter, Tony
Format: Artigo
Jezik:Inglês
Izdano: American Society for Microbiology 2000
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC86069/
https://ncbi.nlm.nih.gov/pubmed/10913175
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