View source for 4lp7


==Crystal structure of the human metapneumovirus matrix protein==
<StructureSection load='4lp7' size='340' side='right' caption='[[4lp7]], [[Resolution|resolution]] 2.83&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lp7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hmpv Hmpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LP7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LP7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=162145 HMPV])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lp7 OCA], [http://pdbe.org/4lp7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lp7 RCSB], [http://www.ebi.ac.uk/pdbsum/4lp7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lp7 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The matrix protein (M) of paramyxoviruses plays a key role in determining virion morphology by directing viral assembly and budding. Here, we report the crystal structure of the human metapneumovirus M at 2.8 A resolution in its native dimeric state. The structure reveals the presence of a high-affinity Ca2+ binding site. Molecular dynamics simulations (MDS) predict a secondary lower-affinity site that correlates well with data from fluorescence-based thermal shift assays. By combining small-angle X-ray scattering with MDS and ensemble analysis, we captured the structure and dynamics of M in solution. Our analysis reveals a large positively charged patch on the protein surface that is involved in membrane interaction. Structural analysis of DOPC-induced polymerization of M into helical filaments using electron microscopy leads to a model of M self-assembly. The conservation of the Ca2+ binding sites suggests a role for calcium in the replication and morphogenesis of pneumoviruses.

Structure and Self-Assembly of the Calcium Binding Matrix Protein of Human Metapneumovirus.,Leyrat C, Renner M, Harlos K, Huiskonen JT, Grimes JM Structure. 2013 Dec 3. pii: S0969-2126(13)00425-5. doi:, 10.1016/j.str.2013.10.013. PMID:24316400<ref>PMID:24316400</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hmpv]]
[[Category: Grimes, J M]]
[[Category: Harlos, K]]
[[Category: Leyrat, C]]
[[Category: Calcium binding protein]]
[[Category: Lipid binding]]
[[Category: Twisted beta sandwich]]
[[Category: Viral matrix]]