Large-scale structural analysis of the classical human protein tyrosine phosphatome.

Journal article

Protein tyrosine phosphatases (PTPs) play a critical role in regulating cellular functions by selectively dephosphorylating their substrates. Here we present 22 human PTP crystal structures that, together with prior structural knowledge, enable a comprehensive analysis of the classical PTP family. Despite their largely conserved fold, surface properties of PTPs are strikingly diverse. A potential secondary substrate-binding pocket is frequently found in phosphatases, and this has implications...

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Authors: Barr, A; Ugochukwu, E; Lee, W; King, O; Filippakopoulos, P

• Publication status: Published
• Journal: Cell
• Volume: 136
• Issue: 2
• Pages: 352-363
• Publication date: 2009-01-01
• DOI: 10.1016/j.cell.2008.11.038
• EISSN: 1097-4172
• ISSN: 0092-8674
• Language: English
• Keywords: Amino Acid Sequence; Structure-Activity Relationship; Crystallography, X-Ray; Models, Molecular; Protein Tyrosine Phosphatases; Humans; Dimerization; Sequence Alignment; Protein Structure, Tertiary