2UV3

Structure of the signal-regulatory protein (SIRP) alpha domain that binds CD47.

2UV3 の概要

• エントリーDOI: 10.2210/pdb2uv3/pdb
• 分子名称: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE SUBSTRATE 1, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: 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
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28805.98

構造登録者

Hatherley, D.,Harlos, K.,Dunlop, D.C.,Stuart, D.I.,Barclay, A.N. (登録日: 2007-03-08, 公開日: 2007-03-27, 最終更新日: 2024-11-06)

主引用文献

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

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: 17369261
DOI: 10.1074/JBC.M611511200

実験手法

X-RAY DIFFRACTION (1.8 Å)