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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| Publicado no: | Mol Cell Biol |
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| Principais autores: | , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Taylor & Francis
2000
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC86069/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10913175/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/mcb.20.16.5917-5929.2000 |
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