- Abstract:
-
The sequence selectivity of 14 classical protein-tyrosine phosphatases (PTPs) (PTPRA, PTPRB, PTPRC, PTPRD, PTPRO, PTP1B, SHP-1, SHP-2, HePTP, PTP-PEST, TCPTP, PTPH1, PTPD1, and PTPD2) was systematically profiled by screening their catalytic domains against combinatorial peptide libraries. All of the PTPs exhibit similar preference for pY peptides rich in acidic amino acids and disfavor positively charged sequences but differ vastly in their degrees of preference/disfavor. Some PTPs (PTP-PEST,...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/bi401223r
-
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- Journal:
- Biochemistry
- Volume:
- 53
- Issue:
- 2
- Pages:
- 397-412
- Publication date:
- 2014-01-05
- DOI:
- EISSN:
-
1520-4995
- ISSN:
-
0006-2960
- URN:
-
uuid:3be889f5-8aaa-45b1-8112-3f50cea58190
- Source identifiers:
-
448195
- Local pid:
- pubs:448195
- Copyright date:
- 2014
Journal article
Diverse levels of sequence selectivity and catalytic efficiency of protein-tyrosine phosphatases.
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