Matches in UGent Biblio for { <https://biblio.ugent.be/publication/2103110#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B355238.
- aggregation creator B355239.
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- aggregation creator B355242.
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- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 2103110.bibtex.
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- aggregation isPartOf urn:issn:0006-4971.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex".
- aggregation abstract "The class III receptor tyrosine kinase (RTKIII) Fms-like tyrosine kinase receptor 3 (Flt3) and its cytokine ligand (FL) play central roles in hematopoiesis and the immune system, by establishing signaling cascades crucial for the development and homeostasis of hematopoietic progenitors and antigen-presenting dendritic cells. However, Flt3 is also one of the most frequently mutated receptors in hematologic malignancies and is currently a major prognostic factor and clinical target for acute myeloid leukemia. Here, we report the structural basis for the Flt3 ligand-receptor complex and unveil an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date. FL induces dimerization of Flt3 via a remarkably compact binding epitope localized at the tip of extracellular domain 3 of Flt3, and it invokes a ternary complex devoid of homotypic receptor interactions. Comparisons of Flt3 with homologous receptors and available mutagenesis data for FL have allowed us to rationalize the unique features of the Flt3 extracellular assembly. Furthermore, thermodynamic dissection of complex formation points to a pronounced enthalpically driven binding event coupled to an entropic penalty. Together, our data suggest that the high-affinity Flt3: FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.".
- aggregation authorList BK654895.
- aggregation endPage "68".
- aggregation issue "1".
- aggregation startPage "60".
- aggregation volume "118".
- aggregation aggregates 2103466.
- aggregation isDescribedBy 2103110.
- aggregation similarTo blood-2011-01-329532.
- aggregation similarTo LU-2103110.