Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots

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 α-helical bundles. Comparisons of structure-function relationships...

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Veröffentlicht in:	Nature structural & molecular biology 2000-06, Vol.7 (6), p.486-491
Hauptverfasser:	Andrew Karplus, P, Savvides, Savvas N, Boone, Tom
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites Bone marrow Colony-stimulating factor Consensus Sequence - genetics Crystal structure Crystallography, X-Ray Cystine Cystine - chemistry Cystine - metabolism Cytokines Dimerization Feature recognition FLT3L protein fms-Like Tyrosine Kinase 3 Growth hormones Hematopoiesis Homology Humans Kinases Knots Ligands Macrophage Colony-Stimulating Factor - chemistry Macrophage Colony-Stimulating Factor - metabolism Macrophages Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Models, Molecular Molecular Sequence Data Mutation - genetics Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - metabolism Protein Structure, Secondary Protein Structure, Tertiary Protein-tyrosine kinase receptors Proto-Oncogene Proteins - chemistry Proto-Oncogene Proteins - metabolism Receptor Protein-Tyrosine Kinases - chemistry Receptor Protein-Tyrosine Kinases - metabolism Receptors Receptors, Platelet-Derived Growth Factor - chemistry Receptors, Platelet-Derived Growth Factor - metabolism Sequence Alignment Stem cell factor Stem Cell Factor - chemistry Stem Cell Factor - metabolism Stem cells Structure-Activity Relationship Structure-function relationships Tyrosine
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