Dimerization of sSCF

Stable Identifier
Reaction [binding]
Homo sapiens
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sSCF exists as noncovalently associated homodimer composed of two monomers interacting head-to-head to form an elongated, slightly bent dimer. Dimerization of sSCF is a dynamic process and it may play a regulatory role in the dimerization and activation of KIT (Zhang et al, 2000; Philo et al, 1996).

Literature References
PubMed ID Title Journal Year
10884405 Crystal structure of human stem cell factor: implication for stem cell factor receptor dimerization and activation

Zhang, Z, Zhang, R, Joachimiak, A, Schlessinger, J, Kong, XP

Proc Natl Acad Sci U S A 2000
8636116 Human stem cell factor dimer forms a complex with two molecules of the extracellular domain of its receptor, Kit

Philo, JS, Wen, J, Wypych, J, Schwartz, MG, Mendiaz, EA, Langley, KE

J Biol Chem 1996
Participant Of
Orthologous Events
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