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4BHV

Measles virus phosphoprotein tetramerization domain

Summary for 4BHV
Entry DOI10.2210/pdb4bhv/pdb
DescriptorPHOSPHOPROTEIN, ACETATE ION, CALCIUM ION, ... (4 entities in total)
Functional Keywordsoligomerization domain, viral protein
Biological sourceMEASLES VIRUS
Total number of polymer chains4
Total formula weight30298.19
Authors
Blocquel, D.,Habchi, J.,Durand, E.,Sevajol, M.,Ferron, F.,Papageorgiou, N.,Longhi, S. (deposition date: 2013-04-08, release date: 2014-04-09, Last modification date: 2023-12-20)
Primary citationBlocquel, D.,Habchi, J.,Durand, E.,Sevajol, M.,Ferron, F.,Erales, J.,Papageorgiou, N.,Longhi, S.
Coiled-Coil Deformations in Crystal Structures: The Measles Virus Phosphoprotein Multimerization Domain as an Illustrative Example.
Acta Crystallogr.,Sect.D, 70:1589-, 2014
Cited by
PubMed Abstract: The structures of two constructs of the measles virus (MeV) phosphoprotein (P) multimerization domain (PMD) are reported and are compared with a third structure published recently by another group [Communie et al. (2013), J. Virol. 87, 7166-7169]. Although the three structures all have a tetrameric and parallel coiled-coil arrangement, structural comparison unveiled considerable differences in the quaternary structure and unveiled that the three structures suffer from significant structural deformation induced by intermolecular interactions within the crystal. These results show that crystal packing can bias conclusions about function and mechanism based on analysis of a single crystal structure, and they challenge to some extent the assumption according to which coiled-coil structures can be reliably predicted from the amino-acid sequence. Structural comparison also highlighted significant differences in the extent of disorder in the C-terminal region of each monomer. The differential flexibility of the C-terminal region is also supported by size-exclusion chromatography and small-angle X-ray scattering studies, which showed that MeV PMD exists in solution as a dynamic equilibrium between two tetramers of different compaction. Finally, the possible functional implications of the flexibility of the C-terminal region of PMD are discussed.
PubMed: 24914970
DOI: 10.1107/S139900471400234X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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数据于2025-07-02公开中

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