2YKD

Structure of the matrix protein from human respiratory syncytial virus

Summary for 2YKD

• Entry DOI: 10.2210/pdb2ykd/pdb
• Related: 2VQP
• Descriptor: MATRIX PROTEIN, ACETATE ION (3 entities in total)
• Functional Keywords: viral protein, viral matrix protein, peripheral membrane protein, virion
• Biological source: HUMAN RESPIRATORY SYNCYTIAL VIRUS
• Total number of polymer chains: 1
• Total formula weight: 28979.58

Authors

McPhee, H.K.,Carlisle, J.L.,Beeby, A.,Money, V.A.,Watson, S.M.D.,Yeo, R.P.,Sanderson, J.M. (deposition date: 2011-05-26, release date: 2011-06-08, Last modification date: 2023-12-20)

Primary citation

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

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

Experimental method

X-RAY DIFFRACTION (1.86 Å)