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2YKT

Crystal structure of the I-BAR domain of IRSp53 (BAIAP2) in complex with an EHEC derived Tir peptide

2YKT の概要
エントリーDOI10.2210/pdb2ykt/pdb
関連するPDBエントリー1WDZ 1Y2O
分子名称BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN 2, TRANSLOCATED INTIMIN RECEPTOR PROTEIN, SULFATE ION, ... (4 entities in total)
機能のキーワードsignaling protein, npy motif, binding pocket
由来する生物種HOMO SAPIENS (HUMAN)
詳細
細胞内の位置Cytoplasm: Q9UQB8
タンパク質・核酸の鎖数2
化学式量合計30237.31
構造登録者
主引用文献De Groot, J.C.,Schluter, K.,Carius, Y.,Quedenau, C.,Vingadassalom, D.,Faix, J.,Weiss, S.M.,Reichelt, J.,Standfuss-Gabisch, C.,Lesser, C.F.,Leong, J.M.,Heinz, D.W.,Bussow, K.,Stradal, T.E.B.
Structural Basis for Complex Formation between Human Irsp53 and the Translocated Intimin Receptor Tir of Enterohemorrhagic E. Coli.
Structure, 19:1294-, 2011
Cited by
PubMed Abstract: Actin assembly beneath enterohemorrhagic E. coli (EHEC) attached to its host cell is triggered by the intracellular interaction of its translocated effector proteins Tir and EspF(U) with human IRSp53 family proteins and N-WASP. Here, we report the structure of the N-terminal I-BAR domain of IRSp53 in complex with a Tir-derived peptide, in which the homodimeric I-BAR domain binds two Tir molecules aligned in parallel. This arrangement provides a protein scaffold linking the bacterium to the host cell's actin polymerization machinery. The structure uncovers a specific peptide-binding site on the I-BAR surface, conserved between IRSp53 and IRTKS. The Tir Asn-Pro-Tyr (NPY) motif, essential for pedestal formation, is specifically recognized by this binding site. The site was confirmed by mutagenesis and in vivo-binding assays. It is possible that IRSp53 utilizes the NPY-binding site for additional interactions with as yet unknown partners within the host cell.
PubMed: 21893288
DOI: 10.1016/J.STR.2011.06.015
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.11 Å)
構造検証レポート
Validation report summary of 2ykt
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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