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Related Experiment Videos

Crystal structure of human stem cell factor: implication for stem cell factor receptor dimerization and activation.

Z Zhang1, R Zhang, A Joachimiak

  • 1Departments of Pharmacology and Biochemistry and Skirball Institute, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.

Proceedings of the National Academy of Sciences of the United States of America
|July 8, 2000
PubMed
Summary

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This study reveals the crystal structure of stem cell factor (SCF), a key protein in cell development. The findings elucidate SCF

Area of Science:

  • Structural Biology
  • Cell Signaling
  • Hematopoiesis Research

Background:

  • Stem cell factor (SCF) is crucial for hematopoiesis and the development of mast cells, melanocytes, and germ cells.
  • SCF exerts its biological functions by activating the c-kit receptor tyrosine kinase.

Purpose of the Study:

  • To determine the crystal structure of the functional core of recombinant human SCF.
  • To elucidate the structural basis of SCF dimerization and its interaction with the c-kit receptor.

Main Methods:

  • X-ray crystallography was used to obtain the 2.3-Å crystal structure of human SCF.
  • Structural analysis focused on identifying key interactions mediating dimerization and potential receptor-binding sites.

Main Results:

Related Experiment Videos

  • The crystal structure reveals SCF as a noncovalent homodimer, with each protomer adopting an antiparallel four-helix bundle fold.
  • Extensive polar and nonpolar interactions stabilize the dimer, featuring a large buried surface area.
  • A hydrophobic crevice and a charged region on each protomer were identified as potential receptor-binding sites.

Conclusions:

  • The determined structure provides insights into the molecular mechanisms of SCF dimerization.
  • The identified potential receptor-binding sites offer a basis for understanding SCF-c-kit complex formation.
  • A model for SCF-c-kit complex formation and dimerization has been proposed based on these structural findings.