Phosphopeptide binding to the N-SH2 domain of tyrosine phosphatase SHP2 correlates with the unzipping of its central β-sheet
SHP2 is a tyrosine phosphatase that plays a regulatory role in multiple intracellular signaling cascades and is known to be oncogenic in certain contexts. In the absence of effectors, SHP2 adopts an autoinhibited conformation with its N-SH2 domain blocking the active site. Given the key role of N-SH...
Kaydedildi:
| Asıl Yazarlar: | , , , , |
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| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
American Association for the Advancement of Science (AAAS)
2024-12-01
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| Seri Bilgileri: | Computational and Structural Biotechnology Journal |
| Konular: | |
| Online Erişim: | http://www.sciencedirect.com/science/article/pii/S2001037024000473 |
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