2YD2

Crystal structure of the N-terminal Ig1-2 module of Human Receptor Protein Tyrosine Phosphatase Sigma

2YD2 の概要

• エントリーDOI: 10.2210/pdb2yd2/pdb
• 関連するPDBエントリー: 2FH7 2YD1 2YD3 2YD4 2YD5 2YD6 2YD7 2YD8 2YD9
• 分子名称: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE S, CHLORIDE ION, IODIDE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: Q13332
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24324.59

構造登録者

Coles, C.H.,Shen, Y.,Tenney, A.P.,Siebold, C.,Sutton, G.C.,Lu, W.,Gallagher, J.T.,Jones, E.Y.,Flanagan, J.G.,Aricescu, A.R. (登録日: 2011-03-17, 公開日: 2011-04-13, 最終更新日: 2024-10-23)

主引用文献

Coles, C.H.,Shen, Y.,Tenney, A.P.,Siebold, C.,Sutton, G.C.,Lu, W.,Gallagher, J.T.,Jones, E.Y.,Flanagan, J.G.,Aricescu, A.R.
Proteoglycan-Specific Molecular Switch for Rptp Sigma Clustering and Neuronal Extension.
Science, 332:484-, 2011

PubMed Abstract: Heparan and chondroitin sulfate proteoglycans (HSPGs and CSPGs, respectively) regulate numerous cell surface signaling events, with typically opposite effects on cell function. CSPGs inhibit nerve regeneration through receptor protein tyrosine phosphatase sigma (RPTPσ). Here we report that RPTPσ acts bimodally in sensory neuron extension, mediating CSPG inhibition and HSPG growth promotion. Crystallographic analyses of a shared HSPG-CSPG binding site reveal a conformational plasticity that can accommodate diverse glycosaminoglycans with comparable affinities. Heparan sulfate and analogs induced RPTPσ ectodomain oligomerization in solution, which was inhibited by chondroitin sulfate. RPTPσ and HSPGs colocalize in puncta on sensory neurons in culture, whereas CSPGs occupy the extracellular matrix. These results lead to a model where proteoglycans can exert opposing effects on neuronal extension by competing to control the oligomerization of a common receptor.

PubMed: 21454754
DOI: 10.1126/SCIENCE.1200840

実験手法

X-RAY DIFFRACTION (2.552 Å)