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Article

Intramolecular hydrophobic interactions are critical mediators of STAT5 dimerization.

Scientific reports - 18 Oct 2016

Fahrenkamp Dirk, Li Jinyu, Ernst Sabrina, Schmitz-Van de Leur Hildegard, Chatain Nicolas, Küster Andrea, Koschmieder Steffen, Lüscher Bernhard, Rossetti Giulia, Müller-Newen Gerhard

Abstract excerpt

STAT5 is an essential transcription factor in hematopoiesis, which is activated through tyrosine phosphorylation in response to cytokine stimulation. Constitutive activation of STAT5 is a hallmark of myeloid and lymphoblastic leukemia. Using homology modeling and molecular dynamics simulations, a model of the STAT5 phosphotyrosine-SH2 domain interface was generated providing first structural information on the...

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Share to Hydrophobic and Hydrophilic Interactions
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 27752093
DOI: 10.1038/srep35454
PMCID: PMC5067585

Provenance

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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