1ETE
CRYSTAL STRUCTURE OF THE FLT3 LIGAND
Summary for 1ETE
| Entry DOI | 10.2210/pdb1ete/pdb |
| Descriptor | FLT3 LIGAND, ZINC ION (3 entities in total) |
| Functional Keywords | four-helix bundle, cytokine |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: P49771 |
| Total number of polymer chains | 4 |
| Total formula weight | 62371.55 |
| Authors | Savvides, S.N.,Boone, T.,Karplus, P.A. (deposition date: 2000-04-12, release date: 2000-06-14, Last modification date: 2024-11-06) |
| Primary citation | Savvides, S.N.,Boone, T.,Andrew Karplus, P. Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots. Nat.Struct.Biol., 7:486-491, 2000 Cited by PubMed Abstract: 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. PubMed: 10881197DOI: 10.1038/75896 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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