2uv3
From Proteopedia
STRUCTURE OF THE SIGNAL-REGULATORY PROTEIN (SIRP) ALPHA DOMAIN THAT BINDS CD47.
Overview
Signal regulatory protein (SIRP) alpha is a membrane receptor that sends inhibitory signals to myeloid cells by engagement of CD47. The high resolution x-ray structure of the N-terminal ligand binding domain shows it to have a distinctive immunoglobulin superfamily V-like fold. Site-directed mutagenesis suggests that CD47 is bound at a surface involving the BC, FG, and DE loops, which distinguishes it from other immunoglobulin superfamily surface proteins that use the faces of the fold, but resembles antigen receptors. The SIRP interaction is confined to a single domain, and its use of an extended DE loop strengthens the similarity with T cell receptor binding and the suggestion that they are closely related in evolution. The employment of loops to form the CD47-binding surface provides a mechanism for small sequence changes to modulate binding specificity, explaining the different binding properties of SIRP family members.
About this Structure
2UV3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of the macrophage signal regulatory protein alpha (SIRPalpha) inhibitory receptor reveals a binding face reminiscent of that used by T cell receptors., Hatherley D, Harlos K, Dunlop DC, Stuart DI, Barclay AN, J Biol Chem. 2007 May 11;282(19):14567-75. Epub 2007 Mar 16. PMID:17369261 Page seeded by OCA on Sun May 4 17:33:02 2008
Categories: Homo sapiens | Single protein | Barclay, A N. | Dunlop, D C. | Harlos, K. | Hatherley, D. | Stuart, D I. | Alternative splicing | Cd47-binding domain of sirp-alpha | Glycoprotein | Human sirp-alpha n terminal v domain | Immunoglobulin domain | Membrane | Phosphorylation | Polymorphism | Receptor | Sh3-binding | Signal-regulatory protein alpha | Transmembrane
