3lqe

<StructureSection load='3lqe' size='340' side='right' caption='[[3lqe]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[3lqe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Murine_norovirus_1 Murine norovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LQE FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lq6|3lq6]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">223997 [NCBI] ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=223997 Murine norovirus 1])</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=3lqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lqe OCA], [http://pdbe.org/3lqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lqe RCSB], [http://www.ebi.ac.uk/pdbsum/3lqe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lqe ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Murine noroviruses (MNV) are closely related to the human noroviruses (HuNoV), which cause the majority of nonbacterial gastroenteritis. Unlike HuNoV, MNV grow in culture and in a small-animal model that represents a tractable model to study norovirus biology. To begin a detailed investigation of molecular events that occur during norovirus binding to cells, the crystallographic structure of the murine norovirus 1 (MNV-1) capsid protein protruding (P) domain has been determined. Crystallization of the bacterially expressed protein yielded two different crystal forms (Protein Data Bank identifiers [PDB ID], 3LQ6 and 3LQE). Comparison of the structures indicated a large degree of structural mobility in loops on the surface of the P2 subdomain. Specifically, the A'-B' and E'-F' loops were found in open and closed conformations. These regions of high mobility include the known escape mutation site for the neutralizing antibody A6.2 and an attenuation mutation site, which arose after serial passaging in culture and led to a loss in lethality in STAT1(-/-) mice, respectively. Modeling of a Fab fragment and crystal structures of the P dimer into the cryoelectron microscopy three-dimensional (3D) image reconstruction of the A6.2/MNV-1 complex indicated that the closed conformation is most likely bound to the Fab fragment and that the antibody contact is localized to the A'-B' and E'-F' loops. Therefore, we hypothesize that these loop regions and the flexibility of the P domains play important roles during MNV-1 binding to the cell surface.

High-resolution x-ray structure and functional analysis of the murine norovirus 1 capsid protein protruding domain.,Taube S, Rubin JR, Katpally U, Smith TJ, Kendall A, Stuckey JA, Wobus CE J Virol. 2010 Jun;84(11):5695-705. Epub 2010 Mar 24. PMID:20335262<ref>PMID:20335262</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 3lqe" style="background-color:#fffaf0;"></div>

*[[Virus coat protein|Virus coat protein]]

[[Category: Rubin, J R]]

[[Category: Stuckey, J A]]

[[Category: Viral protein]]