1I3Z

MURINE EAT2 SH2 DOMAIN IN COMPLEX WITH SLAM PHOSPHOPEPTIDE

1I3Z の概要

• エントリーDOI: 10.2210/pdb1i3z/pdb
• 関連するPDBエントリー: 1d1z 1d4t 1d4w
• 分子名称: EWS/FLI1 ACTIVATED TRANSCRIPT 2, SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE (3 entities in total)
• 機能のキーワード: sh2 domain phosphotyrosine signal transduction lymphocyte, signaling protein
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13499.63

構造登録者

Lu, J.,Poy, F.,Morra, M.,Terhorst, C.,Eck, M.J. (登録日: 2001-02-19, 公開日: 2003-04-08, 最終更新日: 2024-11-13)

主引用文献

Morra, M.,Lu, J.,Poy, F.,Martin, M.,Sayos, J.,Calpe, S.,Gullo, C.,Howie, D.,Rietdijk, S.,Thompson, A.,Coyle, A.J.,Denny, C.,Yaffe, M.B.,Engel, P.,Eck, M.J.,Terhorst, C.
Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells.
Eur.J.Biochem., 20:5840-5852, 2001

PubMed Abstract: The T and natural killer (NK) cell-specific gene SAP (SH2D1A) encodes a 'free SH2 domain' that binds a specific tyrosine motif in the cytoplasmic tail of SLAM (CD150) and related cell surface proteins. Mutations in SH2D1A cause the X-linked lymphoproliferative disease, a primary immunodeficiency. Here we report that a second gene encoding a free SH2 domain, EAT-2, is expressed in macrophages and B lympho cytes. The EAT-2 structure in complex with a phosphotyrosine peptide containing a sequence motif with Tyr281 of the cytoplasmic tail of CD150 is very similar to the structure of SH2D1A complexed with the same peptide. This explains the high affinity of EAT-2 for the pTyr motif in the cytoplasmic tail of CD150 but, unlike SH2D1A, EAT-2 does not bind to non-phosphorylated CD150. EAT-2 binds to the phosphorylated receptors CD84, CD150, CD229 and CD244, and acts as a natural inhibitor, which interferes with the recruitment of the tyrosine phosphatase SHP-2. We conclude that EAT-2 plays a role in controlling signal transduction through at least four receptors expressed on the surface of professional antigen-presenting cells.

PubMed: 11689425
DOI: 10.1093/emboj/20.21.5840

実験手法

X-RAY DIFFRACTION (2.15 Å)