1D4T

CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP IN COMPLEX WITH A SLAM PEPTIDE

1D4T の概要

• エントリーDOI: 10.2210/pdb1d4t/pdb
• 関連するPDBエントリー: 1D1Z 1D4W
• 分子名称: T CELL SIGNAL TRANSDUCTION MOLECULE SAP, SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE (3 entities in total)
• 機能のキーワード: sh2 domain, tyrosine kinase, signal transduction, peptide recognition, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm : O60880; Cell membrane ; Single-pass type I membrane protein. Isoform 3: Secreted . Isoform 4: Cell membrane : Q13291
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12982.91

構造登録者

Poy, F.,Yaffe, M.B.,Sayos, J.,Saxena, K.,Eck, M.J. (登録日: 1999-10-06, 公開日: 1999-10-14, 最終更新日: 2024-02-07)

主引用文献

Poy, F.,Yaffe, M.B.,Sayos, J.,Saxena, K.,Morra, M.,Sumegi, J.,Cantley, L.C.,Terhorst, C.,Eck, M.J.
Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition.
Mol.Cell, 4:555-561, 1999

PubMed Abstract: SAP, the product of the gene mutated in X-linked lymphoproliferative syndrome (XLP), consists of a single SH2 domain that has been shown to bind the cytoplasmic tail of the lymphocyte coreceptor SLAM. Here we describe structures that show that SAP binds phosphorylated and nonphosphorylated SLAM peptides in a similar mode, with the tyrosine or phosphotyrosine residue inserted into the phosphotyrosine-binding pocket. We find that specific interactions with residues N-terminal to the tyrosine, in addition to more characteristic C-terminal interactions, stabilize the complexes. A phosphopeptide library screen and analysis of mutations identified in XLP patients confirm that these extended interactions are required for SAP function. Further, we show that SAP and the similar protein EAT-2 recognize the sequence motif TIpYXX(V/I).

PubMed: 10549287
DOI: 10.1016/S1097-2765(00)80206-3

実験手法

X-RAY DIFFRACTION (1.1 Å)