1EXZ

STRUCTURE OF STEM CELL FACTOR

Summary for 1EXZ

• Entry DOI: 10.2210/pdb1exz/pdb
• Descriptor: STEM CELL FACTOR, CALCIUM ION, SAMARIUM (III) ION, ... (5 entities in total)
• Functional Keywords: scf, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cell membrane; Single-pass type I membrane protein (By similarity). Soluble KIT ligand: Secreted: P21583
• Total number of polymer chains: 4
• Total formula weight: 64832.96

Authors

Zhang, Z.,Zhang, R.,Joachimiak, A.,Schlessinger, J.,Kong, X. (deposition date: 2000-05-05, release date: 2000-07-06, Last modification date: 2011-07-13)

Primary citation

Zhang, Z.,Zhang, R.,Joachimiak, A.,Schlessinger, J.,Kong, X.P.
Crystal structure of human stem cell factor: implication for stem cell factor receptor dimerization and activation.
Proc.Natl.Acad.Sci.USA, 97:7732-7737, 2000

PubMed Abstract: Stem cell factor (SCF) plays important roles in hematopoiesis and the survival, proliferation, and differentiation of mast cells, melanocytes, and germ cells. SCF mediates its biological effects by binding to and activating a receptor tyrosine kinase designated c-kit or SCF receptor. In this report we describe the 2.3-A crystal structure of the functional core of recombinant human SCF. SCF is a noncovalent homodimer composed of two slightly wedged protomers. Each SCF protomer exhibits an antiparallel four-helix bundle fold. Dimerization is mediated by extensive polar and nonpolar interactions between the two protomers with a large buried surface area. Finally, we have identified a hydrophobic crevice and a charged region at the tail of each protomer that functions as a potential receptor-binding site. On the basis of these observations, a model for SCF small middle dotc-kit complex formation and dimerization is proposed.

PubMed: 10884405
DOI: 10.1073/pnas.97.14.7732

Experimental method

X-RAY DIFFRACTION (2.3 Å)