7V6Y
Cryo-EM structure of Patched in lipid nanodisc - the wildtype, 3.5 angstrom (re-processed with dataset of 7dzq)
「7DZQ」から置き換えられました7V6Y の概要
| エントリーDOI | 10.2210/pdb7v6y/pdb |
| EMDBエントリー | 31753 |
| 分子名称 | Protein patched homolog 1,Protein patched homolog 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CHOLESTEROL, ... (5 entities in total) |
| 機能のキーワード | caveolae, hedgehog signaling, lipid nanodisc, patched, ptc1 dimer, membrane protein |
| 由来する生物種 | Mus musculus (Mouse) 詳細 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 123980.42 |
| 構造登録者 | |
| 主引用文献 | Luo, Y.,Wan, G.,Zhang, X.,Zhou, X.,Wang, Q.,Fan, J.,Cai, H.,Ma, L.,Wu, H.,Qu, Q.,Cong, Y.,Zhao, Y.,Li, D. Cryo-EM study of patched in lipid nanodisc suggests a structural basis for its clustering in caveolae. Structure, 29:1286-, 2021 Cited by PubMed Abstract: The 12-transmembrane protein Patched (Ptc1) acts as a suppressor for Hedgehog (Hh) signaling by depleting sterols in the cytoplasmic membrane leaflet that are required for the activation of downstream regulators. The positive modulator Hh inhibits Ptc1's transporter function by binding to Ptc1 and its co-receptors, which are locally concentrated in invaginated microdomains known as caveolae. Here, we reconstitute the mouse Ptc1 into lipid nanodiscs and determine its structure using single-particle cryoelectron microscopy. The structure is overall similar to those in amphipol and detergents but displays various conformational differences in the transmembrane region. Although most particles show monomers, we observe Ptc1 dimers with distinct interaction patterns and different membrane curvatures, some of which are reminiscent of caveolae. We find that an extramembranous "hand-shake" region rich in hydrophobic and aromatic residues mediates inter-Ptc1 interactions under different membrane curvatures. Our data provide a plausible framework for Ptc1 clustering in the highly curved caveolae. PubMed: 34174188DOI: 10.1016/j.str.2021.06.004 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.5 Å) |
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