4YX2

Crystal structure of Bovine prion protein complexed with POM1 FAB

4YX2 の概要

• エントリーDOI: 10.2210/pdb4yx2/pdb
• 関連するPDBエントリー: 4H88 4YXH 4YXK 4YXL
• 分子名称: Major prion protein, POM1 FAB HEAVY CHAIN, POM1 FAB LIGHT CHAIN, ... (4 entities in total)
• 機能のキーワード: prion, antibody, complex, immune system complex, immune system
• 由来する生物種: Bos taurus (Bovine); 詳細
• 細胞内の位置: Cell membrane ; Lipid-anchor, GPI-anchor : P10279
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 65395.37

構造登録者

Baral, P.K.,Swayampakula, M.,James, M.N.G. (登録日: 2015-03-22, 公開日: 2015-09-23, 最終更新日: 2024-11-06)

主引用文献

Baral, P.K.,Swayampakula, M.,Aguzzi, A.,James, M.N.
X-ray structural and molecular dynamical studies of the globular domains of cow, deer, elk and Syrian hamster prion proteins.
J.Struct.Biol., 192:37-47, 2015

PubMed Abstract: Misfolded prion proteins are the cause of neurodegenerative diseases that affect many mammalian species, including humans. Transmission of the prion diseases poses a considerable public-health risk as a specific prion disease such as bovine spongiform encephalopathy can be transferred to humans and other mammalian species upon contaminant exposure. The underlying mechanism of prion propagation and the species barriers that control cross species transmission has been investigated quite extensively. So far a number of prion strains have been characterized and those have been intimately linked to species-specific infectivity and other pathophysiological manifestations. These strains are encoded by a protein-only agent, and have a high degree of sequence identity across mammalian species. The molecular events that lead to strain differentiation remain elusive. In order to contribute to the understanding of strain differentiation, we have determined the crystal structures of the globular, folded domains of four prion proteins (cow, deer, elk and Syrian hamster) bound to the POM1 antibody fragment Fab. Although the overall structural folds of the mammalian prion proteins remains extremely similar, there are several local structural variations observed in the misfolding-initiator motifs. In additional molecular dynamics simulation studies on these several prion proteins reveal differences in the local fluctuations and imply that these differences have possible roles in the unfolding of the globular domains. These local variations in the structured domains perpetuate diverse patterns of prion misfolding and possibly facilitate the strain selection and adaptation.

PubMed: 26320075
DOI: 10.1016/j.jsb.2015.08.014

実験手法

X-RAY DIFFRACTION (2.194 Å)