2UV3
Structure of the signal-regulatory protein (SIRP) alpha domain that binds CD47.
Summary for 2UV3
| Entry DOI | 10.2210/pdb2uv3/pdb |
| Descriptor | TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE SUBSTRATE 1, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | cd47-binding domain of sirp-alpha, receptor, membrane, sh3- binding, glycoprotein, transmembrane, phosphorylation, human sirp-alpha n terminal v domain, immunoglobulin domain, signal-regulatory protein alpha |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 2 |
| Total formula weight | 28805.98 |
| Authors | Hatherley, D.,Harlos, K.,Dunlop, D.C.,Stuart, D.I.,Barclay, A.N. (deposition date: 2007-03-08, release date: 2007-03-27, Last modification date: 2024-11-06) |
| Primary citation | Hatherley, D.,Harlos, K.,Dunlop, D.C.,Stuart, D.I.,Barclay, A.N. The Structure of the Macrophage Signal Regulatory Protein Alpha (Sirpalpha) Inhibitory Receptor Reveals a Binding Face Reminiscent of that Used by T Cell Receptors. J.Biol.Chem., 282:14567-, 2007 Cited by PubMed Abstract: 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. PubMed: 17369261DOI: 10.1074/JBC.M611511200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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