SIRP alpha binds CD47

Stable Identifier
Reaction [binding]
Homo sapiens
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CD47 is an extracellular ligand for SIRP alpha. SIRP alpha directly binds to the loops of the Ig variable like domain of CD47 in an end-to-end fashion. The SIRP alpha/CD47 interaction is unusual in that it can lead to bidirectional signaling through SIRP alpha and CD47. The major function of this interaction is prevention of phagocytosis of RBC and platelets by macrophages.
Literature References
PubMed ID Title Journal Year
18657508 Paired receptor specificity explained by structures of signal regulatory proteins alone and complexed with CD47

Harlos, K, Barclay, AN, Graham, SC, Stuart, DI, Turner, J, Hatherley, D

Mol Cell 2008
17070842 Functional elements on SIRPalpha IgV domain mediate cell surface binding to CD47

Zhou, Y, Tong, Q, Liu, Y, Chen, Y-T, Buhring, HJ, Zen, K, Ha, B, Lee, HW, Yang, Y, Chen, CX, Yang, JJ

J Mol Biol 2007
19628875 Structure of signal-regulatory protein alpha: a link to antigen receptor evolution

Harlos, K, Barclay, AN, Graham, SC, Stuart, DI, Hatherley, D

J Biol Chem 2009
17369261 The structure of the macrophage signal regulatory protein alpha (SIRPalpha) inhibitory receptor reveals a binding face reminiscent of that used by T cell receptors

Harlos, K, Dunlop, DC, Barclay, AN, Stuart, DI, Hatherley, D

J Biol Chem 2007
10572074 Human signal-regulatory protein is expressed on normal, but not on subsets of leukemic myeloid cells and mediates cellular adhesion involving its counterreceptor CD47

Chen, Z, Cant, C, Brown, EJ, Brugger, W, Buhring, HJ, Kanz, L, Ullrich, A, Rappold, I, Seiffert, M

Blood 1999
Orthologous Events
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