Protein assembly mediated by sulfonatocalix[4]arene

A crystal structure of lysozyme in complex with p-sulfonato-calix[4]arene (sclx4) reveals a linear assembly of protein tetramers glued together by protein-calixarene interactions. One interaction involves encapsulation of the highly exposed C-terminal Arg128. The other involves an intricate protein-...

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Bibliographic Details
Published inChemical communications (Cambridge, England) Vol. 50; no. 72; pp. 10412 - 10415
Main Authors McGovern, Róise E, McCarthy, Andrew A, Crowley, Peter B
Format Journal Article
LanguageEnglish
Published England 01.01.2014
Subjects
Assembly
Binding Sites
Calixarenes - chemistry
Calixarenes - metabolism
Crystal structure
Crystallography, X-Ray
Encapsulation
Exposure
Fragmentation
Lysozyme
Molecular Dynamics Simulation
Muramidase - chemistry
Muramidase - metabolism
Phenols - chemistry
Phenols - metabolism
Polyethylene glycol
Polyethylene Glycols - chemistry
Polyethylene Glycols - metabolism
Protein Binding
Protein Structure, Quaternary
Proteins
Sulfonic Acids - chemistry
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Summary:A crystal structure of lysozyme in complex with p-sulfonato-calix[4]arene (sclx4) reveals a linear assembly of protein tetramers glued together by protein-calixarene interactions. One interaction involves encapsulation of the highly exposed C-terminal Arg128. The other involves an intricate protein-bound complex of sclx4, Mg(2+) and a fragment of polyethylene glycol.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:1359-7345
1364-548X
DOI:10.1039/c4cc04897k