2N64

NMR Structure of the C-terminal Coiled-Coil Domain of CIN85

2N64 の概要

• エントリーDOI: 10.2210/pdb2n64/pdb
• 関連するPDBエントリー: 5abs
• NMR情報: BMRB: 25750
• 分子名称: SH3 domain-containing kinase-binding protein 1 (1 entity in total)
• 機能のキーワード: signaling protein, adaptor protein, coiled-coil domain, b-cell antigen receptor signaling
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton: Q96B97
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 26286.56

構造登録者

Habeck, M.,Becker, S.,Griesinger, C.,Wong, L.E. (登録日: 2015-08-11, 公開日: 2016-07-13, 最終更新日: 2024-05-01)

主引用文献

Kuhn, J.,Wong, L.E.,Pirkuliyeva, S.,Schulz, K.,Schwiegk, C.,Funfgeld, K.G.,Keppler, S.,Batista, F.D.,Urlaub, H.,Habeck, M.,Becker, S.,Griesinger, C.,Wienands, J.
The adaptor protein CIN85 assembles intracellular signaling clusters for B cell activation.
Sci.Signal., 9:ra66-ra66, 2016

PubMed Abstract: The adaptor molecule Cbl-interacting protein of 85 kD (CIN85) regulates signaling from a number of cell surface receptors, such as growth factor receptors and antigen receptors on lymphocytes. Because of its multidomain structure, CIN85 is thought to act as a classical adaptor protein that connects functionally distinct components of a given signaling pathway through diverse protein domains. However, we found that in B lymphocytes, CIN85 functions to oligomerize SLP-65, which is the central effector protein of the B cell receptor (BCR). Therefore, CIN85 trimerizes through a carboxyl-terminal, coiled-coil domain. The multiple Src homology 3 (SH3) domains of trimeric CIN85 molecules associated with multiple SLP-65 molecules, which recruited further CIN85 trimers, thereby perpetuating the oligomerization process. Formation of this oligomeric signaling complex in resting B cells rendered the cells poised for the efficient initiation of intracellular signaling upon BCR stimulation. Our data suggest that the functionality of signaling cascades does not rely solely on the qualitative linkage of their various components but requires a critical number of effectors to become concentrated in signaling complexes.

PubMed: 27353366
DOI: 10.1126/scisignal.aad6275

実験手法

SOLUTION NMR