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2JJW

Structure of human signal regulatory protein (sirp) gamma

Summary for 2JJW
Entry DOI10.2210/pdb2jjw/pdb
Related2JJU 2JJV 2UV3
DescriptorSIGNAL REGULATORY PROTEIN GAMMA (2 entities in total)
Functional Keywordsimmunoglobulin domain, immunoglobulin superfamily, sirp, sirpg, membrane, glycoprotein, cell adhesion, signal regulatory protein gamma, transmembrane, paired receptor, alternative splicing
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains1
Total formula weight14213.29
Authors
Hatherley, D.,Graham, S.C.,Turner, J.,Harlos, K.,Stuart, D.I.,Barclay, A.N. (deposition date: 2008-04-22, release date: 2008-08-05, Last modification date: 2024-11-06)
Primary citationHatherley, D.,Graham, S.C.,Turner, J.,Harlos, K.,Stuart, D.I.,Barclay, A.N.
Paired Receptor Specificity Explained by Structures of Signal Regulatory Proteins Alone and Complexed with Cd47.
Mol.Cell, 31:266-, 2008
Cited by
PubMed Abstract: CD47 is a widely distributed cell-surface protein that acts a marker of self through interactions of myeloid and neural cells. We describe the high-resolution X-ray crystallographic structures of the immunoglobulin superfamily domain of CD47 alone and in complex with the N-terminal ligand-binding domain of signal regulatory protein alpha (SIRPalpha). The unusual and convoluted interacting face of CD47, comprising the N terminus and loops at the end of the domain, intercalates with the corresponding regions in SIRPalpha. We have also determined structures of the N-terminal domains of SIRPbeta, SIRPbeta(2), and SIRPgamma; proteins that are closely related to SIRPalpha but bind CD47 with negligible or reduced affinity. These results explain the specificity of CD47 for the SIRP family of paired receptors in atomic detail. Analysis of SIRPalpha polymorphisms suggests that these, as well as the activating SIRPs, may have evolved to counteract pathogen binding to the inhibitory SIRPalpha receptor.
PubMed: 18657508
DOI: 10.1016/J.MOLCEL.2008.05.026
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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