Structural highlights
Function
FLT3L_HUMAN Stimulates the proliferation of early hematopoietic cells by activating FLT3. Synergizes well with a number of other colony stimulating factors and interleukins.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Human Flt3 ligand (Flt3L) stimulates early hematopoiesis by activating a type III tyrosine kinase receptor on primitive bone marrow stem cells. The crystal structure of soluble Flt3L reveals that it is a homodimer of two short chain alpha-helical bundles. Comparisons of structure-function relationships of Flt3L with the homologous hematopoietic cytokines macrophage colony stimulating factor (MCSF) and stem cell factor (SCF) suggest that they have a common receptor binding mode that is distinct from the paradigm derived from the complex of growth hormone with its receptor. Furthermore, we identify recognition features common to all helical and cystine-knot protein ligands that activate type III tyrosine kinase receptors, and the closely related type V tyrosine kinase receptors.
Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots.,Savvides SN, Boone T, Andrew Karplus P Nat Struct Biol. 2000 Jun;7(6):486-91. PMID:10881197[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Savvides SN, Boone T, Andrew Karplus P. Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots. Nat Struct Biol. 2000 Jun;7(6):486-91. PMID:10881197 doi:10.1038/75896
