3BIN

Structure of the DAL-1 and TSLC1 (372-383) complex

3BIN の概要

• エントリーDOI: 10.2210/pdb3bin/pdb
• 関連するPDBエントリー: 2HE7
• 分子名称: Band 4.1-like protein 3, Cell adhesion molecule 1 (3 entities in total)
• 機能のキーワード: ferm domain, dal-1, tslc1, actin-binding, cytoskeleton, phosphoprotein, structural protein, anti-oncogene, apoptosis, cell adhesion, cell cycle, developmental protein, differentiation, glycoprotein, immune response, immunoglobulin domain, membrane, spermatogenesis, transmembrane
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton (By similarity): Q9Y2J2; Cell membrane; Single-pass type I membrane protein: Q9BY67
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34443.37

構造登録者

Busam, R.D.,Arrowsmith, C.H.,Collins, R.,Dahlgren, L.G.,Edwards, A.M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Johansson, A.,Johansson, I.,Kallas, A.,Karlberg, T.,Kotenyova, T.,Lehtio, L.,Moche, M.,Nilsson, M.E.,Nordlund, P.,Nyman, T.,Sagemark, J.,Svensson, L.,Thorsell, A.G.,Tresaugues, L.,Van Den Berg, S.,Weigelt, J.,Welin, M.,Berglund, H.,Persson, C.,Hallberg, B.M. (登録日: 2007-11-30, 公開日: 2008-01-15, 最終更新日: 2024-03-13)

主引用文献

Busam, R.D.,Thorsell, A.-G.,Flores, A.,Hammarstrom, M.,Persson, C.,Obrink, B.,Hallberg, B.M.
Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding to differentially expressed in adenocarcinoma of the lung (DAL-1/4.1B)
J.Biol.Chem., 286:4511-4516, 2011

PubMed Abstract: Perturbed cell adhesion mechanisms are crucial for tumor invasion and metastasis. A cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1), is inactivated in a majority of metastatic cancers. DAL-1 (differentially expressed in adenocarcinoma of the lung protein), another tumor suppressor, binds through its FERM domain to the TSLC1 C-terminal, 4.1 glycophorin C-like, cytoplasmic domain. However, the molecular basis for this interaction is unknown. Here, we describe the crystal structure of a complex between the DAL-1 FERM domain and a portion of the TSLC1 cytoplasmic domain. DAL-1 binds to TSLC1 through conserved residues in a well defined hydrophobic pocket in the structural C-lobe of the DAL-1 FERM domain. From the crystal structure, it is apparent that Tyr(406) and Thr(408) in the TSLC1 cytoplasmic domain form the most important interactions with DAL-1, and this was also confirmed by surface plasmon resonance studies. Our results refute earlier exon deletion experiments that indicated that glycophorin C interacts with the α-lobe of 4.1 FERM domains.

PubMed: 21131357
DOI: 10.1074/jbc.M110.174011

実験手法

X-RAY DIFFRACTION (2.3 Å)