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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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| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
American Society for Microbiology
2000
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC86069/ https://ncbi.nlm.nih.gov/pubmed/10913175 |
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