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Article

Phosphopeptide ligands of the SHP-1 N-SH2 domain: effects on binding and stimulation of phosphatase activity.

ChemMedChem - 1 Aug 2006

Hampel Kornelia, Kaufhold Ina, Zacharias Martin, Böhmer Frank D, Imhof Diana

Abstract excerpt

Src homology 2 (SH2)-domain-mediated interactions with phosphotyrosine (pY)-containing ligands are critical for the regulation of SHP-1 phosphatase activity. Peptides based on a binding site from receptor tyrosine kinase Ros (EGLN-pY2267-MVL, 1) have recently been shown to bind to the SHP-1 N-terminal SH2 domain (N-SH2) with considerably high affinity. In addition, two peptides cyclized between positions -1 and...

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Share to Binding, Competitive
Share to Intracellular Signaling Peptides and Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Peptides, Cyclic

Share to Phosphopeptides

Share to Protein Tyrosine Phosphatase, Non-Receptor Type 6

Share to Protein Tyrosine Phosphatases

Share to src Homology Domains

Source

Identifiers

PMID: 16902940
DOI: 10.1002/cmdc.200600037

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COCH

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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