View source for 4bhv


==Measles virus phosphoprotein tetramerization domain==
<StructureSection load='4bhv' size='340' side='right'caption='[[4bhv]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bhv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Measles_morbillivirus Measles morbillivirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BHV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhv OCA], [https://pdbe.org/4bhv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bhv RCSB], [https://www.ebi.ac.uk/pdbsum/4bhv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bhv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHOSP_MEASA PHOSP_MEASA] Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Coiled-coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative example.,Blocquel D, Habchi J, Durand E, Sevajol M, Ferron F, Erales J, Papageorgiou N, Longhi S Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1589-603. doi:, 10.1107/S139900471400234X. Epub 2014 May 24. PMID:24914970<ref>PMID:24914970</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4bhv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Measles morbillivirus]]
[[Category: Blocquel D]]
[[Category: Durand E]]
[[Category: Ferron F]]
[[Category: Habchi J]]
[[Category: Longhi S]]
[[Category: Papageorgiou N]]
[[Category: Sevajol M]]