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3msh

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{{STRUCTURE_3msh| PDB=3msh | SCENE= }}
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==Crystal structure of Hepatitis B X-Interacting Protein at high resolution==
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===Crystal structure of Hepatitis B X-Interacting Protein at high resolution===
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<StructureSection load='3msh' size='340' side='right' caption='[[3msh]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
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{{ABSTRACT_PUBMED_21059355}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3msh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MSH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MSH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ms6|3ms6]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HBXIP, XIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<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=3msh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3msh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3msh RCSB], [http://www.ebi.ac.uk/pdbsum/3msh PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Hepatitis B X-interacting protein (HBXIP) is a ubiquitous protein that was originally identified as a binding partner of the hepatitis B viral protein HBx. HBXIP is also thought to serve as an anti-apoptotic cofactor of survivin, promoting the suppression of pro-caspase-9 activation. Here were port the crystal structure of the shortest isoform of HBXIP (91 aa long, approximately 11 kDa) at 1.5 A resolution. HBXIP crystal shows a monomer per asymmetric unit, with a profilin-like fold which is common to a super family of proteins, the Roadblock/LC7 domain family involved in protein-protein interactions. Based on this fold, we propose that HBXIP can form a dimer that can indeed be found in the crystal when symmetric molecules are generated around the asymmetric unit. This dimer shows an extended beta-sheet area formed by 10 anti-parallel beta-strands from both subunits. Another interesting aspect of the proposed HBXIP dimer interface is the presence of a small leucine zipper between the two alpha2 helices of each monomer. In solution, the scattering curve obtained by small-angle X-ray scattering for the sample used for crystallization indicates that the protein is dimeric form in solution. The fit between the experimental small angle X-ray scattering curve and the back calculated curves for two potential crystal dimers shows a significant preference for the Roadblock/LC7 fold dimer model. Moreover, the HBXIP crystal structure represents a step towards understanding the cellular role of HBXIP.
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==Function==
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Structural characterization of HBXIP: the protein that interacts with the anti-apoptotic protein survivin and the oncogenic viral protein HBx.,Garcia-Saez I, Lacroix FB, Blot D, Gabel F, Skoufias DA J Mol Biol. 2011 Jan 14;405(2):331-40. Epub 2010 Nov 6. PMID:21059355<ref>PMID:21059355</ref>
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[[http://www.uniprot.org/uniprot/HBXIP_HUMAN HBXIP_HUMAN]] As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. When complexed to BIRC5, interferes with apoptosome assembly, preventing recruitment of pro-caspase-9 to oligomerized APAF1, thereby selectively suppressing apoptosis initiated via the mitochondrial/cytochrome c pathway. Down-regulates hepatitis B virus (HBV) replication.<ref>PMID:12773388</ref> <ref>PMID:22980980</ref>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[3msh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MSH OCA].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:021059355</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Garcia-Saez, I.]]
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[[Category: Garcia-Saez, I]]
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[[Category: Skoufias, D.]]
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[[Category: Skoufias, D]]
[[Category: Alpha-beta protein]]
[[Category: Alpha-beta protein]]
[[Category: Profilin-like fold]]
[[Category: Profilin-like fold]]
[[Category: Protein binding]]
[[Category: Protein binding]]
[[Category: Roadblock/lc7 domain superfamily]]
[[Category: Roadblock/lc7 domain superfamily]]

Revision as of 17:08, 18 December 2014

Crystal structure of Hepatitis B X-Interacting Protein at high resolution

3msh, resolution 1.51Å

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