Thermodynamic and structural description of allosterically regulated VEGF receptor 2 dimerization
نویسندگان
چکیده
Maurice S. Brozzo, Saša Bjelić, Kaisa Kisko, Thomas Schleier, Veli-Matti Leppänen, Kari Alitalo, Fritz K. Winkler and Kurt Ballmer-Hofer Paul Scherrer Institut, Molecular Cell Biology and Biomolecular Research CH-5232 Villigen PSI, Switzerland; Molecular Cancer Biology Program, Biomedicum Helsinki, Department of Pathology, Haartman Institute and Helsinki University Central Hospital, P.O.B. 63, (Haartmaninkatu 8), 00014 University of Helsinki, Finland 1 These authors contributed equally to this work. 2 To whom correspondence should be addressed: Kurt Ballmer-Hofer, Paul Scherrer Institut, Biomolecular Research, Molecular Cell Biology, CH-5232 Villigen PSI, Switzerland; e-mail: [email protected]; phone: +4156 3104165; fax: +4156 3105288
منابع مشابه
Thermodynamic and structural description of allosterically regulated VEGFR-2 dimerization.
VEGFs activate 3 receptor tyrosine kinases, VEGFR-1, VEGFR-2, and VEGFR-3, promoting angiogenic and lymphangiogenic signaling. The extracellular receptor domain (ECD) consists of 7 Ig-homology domains; domains 2 and 3 (D23) represent the ligand-binding domain, whereas the function of D4-7 is unclear. Ligand binding promotes receptor dimerization and instigates transmembrane signaling and recept...
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VEGFs activate 3 receptor tyrosine kinases, VEGFR-1, VEGFR-2, and VEGFR-3, promoting angiogenic and lymphangiogenic signaling. The extracellular receptor domain (ECD) consists of 7 Ig-homology domains; domains 2 and 3 (D23) represent the ligandbinding domain, whereas the function of D4-7 is unclear. Ligand binding promotes receptor dimerization and instigates transmembrane signaling and recepto...
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