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2YKD

Structure of the matrix protein from human respiratory syncytial virus

2YKD の概要
エントリーDOI10.2210/pdb2ykd/pdb
関連するPDBエントリー2VQP
分子名称MATRIX PROTEIN, ACETATE ION (3 entities in total)
機能のキーワードviral protein, viral matrix protein, peripheral membrane protein, virion
由来する生物種HUMAN RESPIRATORY SYNCYTIAL VIRUS
タンパク質・核酸の鎖数1
化学式量合計28979.58
構造登録者
McPhee, H.K.,Carlisle, J.L.,Beeby, A.,Money, V.A.,Watson, S.M.D.,Yeo, R.P.,Sanderson, J.M. (登録日: 2011-05-26, 公開日: 2011-06-08, 最終更新日: 2023-12-20)
主引用文献Mcphee, H.K.,Carlisle, J.L.,Beeby, A.,Money, V.A.,Watson, S.M.D.,Yeo, R.P.,Sanderson, J.M.
Influence of Lipids on the Interfacial Disposition of Respiratory Syncytical Virus Matrix Protein.
Langmuir, 27:304-, 2011
Cited by
PubMed Abstract: The propensity of a matrix protein from an enveloped virus of the Mononegavirales family to associate with lipids representative of the viral envelope has been determined using label-free methods, including tensiometry and Brewster angle microscopy on lipid films at the air-water interface and atomic force microscopy on monolayers transferred to OTS-treated silicon wafers. This has enabled factors that influence the disposition of the protein with respect to the lipid interface to be characterized. In the absence of sphingomyelin, respiratory syncytial virus matrix protein penetrates monolayers composed of mixtures of phosphocholines with phosphoethanolamines or cholesterol at the air-water interface. In ternary mixtures composed of sphingomyelin, 1,2-dioleoyl-sn-glycero-3-phosphocholine, and cholesterol, the protein exhibits two separate behaviors: (1) peripheral association with the surface of sphingomyelin-rich domains and (2) penetration of sphingomyelin-poor domains. Prolonged incubation of the protein with mixtures of phosphocholines and phosphoethanolamines leads to the formation of helical protein assemblies of uniform diameter that demonstrate an inherent propensity of the protein to assemble into a filamentous form.
PubMed: 21141948
DOI: 10.1021/LA104041N
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.86 Å)
構造検証レポート
Validation report summary of 2ykd
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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