1rvf: Difference between revisions
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<StructureSection load='1rvf' size='340' side='right' caption='[[1rvf]], [[Resolution|resolution]] 4.00Å' scene=''> | <StructureSection load='1rvf' size='340' side='right' caption='[[1rvf]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1rvf]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1rvf]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrv-14 Hrv-14], [http://en.wikipedia.org/wiki/Human_rhinovirus Human rhinovirus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The August 2001 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Poliovirus and Rhinovirus'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2001_8 10.2210/rcsb_pdb/mom_2001_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RVF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RVF FirstGlance]. <br> | ||
</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=1rvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rvf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rvf RCSB], [http://www.ebi.ac.uk/pdbsum/1rvf PDBsum]</span></td></tr> | </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=1rvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rvf OCA], [http://pdbe.org/1rvf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rvf RCSB], [http://www.ebi.ac.uk/pdbsum/1rvf PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1rvf" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Hrv-14]] | ||
[[Category: Human rhinovirus | [[Category: Human rhinovirus]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Poliovirus and Rhinovirus]] | [[Category: Poliovirus and Rhinovirus]] |
Revision as of 18:36, 11 September 2015
FAB COMPLEXED WITH INTACT HUMAN RHINOVIRUSFAB COMPLEXED WITH INTACT HUMAN RHINOVIRUS
Structural highlights
Function[POLG_HRV14] Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). The capsid interacts with human ICAM1 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis. VP0 precursor is a component of immature procapsids (By similarity). Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription (By similarity). Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity). Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity). Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity). RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity). Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three-dimensional structure of intact human rhinovirus 14 (HRV-14) complexed with Fab fragments (Fab17-IA) from a strongly neutralizing antibody that binds bivalently to the virion has been determined to 4.0 angstrom resolution by a combination of X-ray crystallography and cryo-electron microscopy. In contradiction to the most commonly held model of antibody-mediated neutralization, Fab17-IA does not induce a conformational change in the HRV-14 capsid. Instead, the paratope of the antibody undergoes a large conformational change to accommodate the epitope. Unlike any previously described antibody-antigen structure, the conserved framework region of the antibody makes extensive contact with the viral surface. Fab17-IA penetrates deep within the canyon in which the cellular receptor for HRV-14 binds. Hence, it is unlikely that viral quaternary structure evolves merely to evade immune recognition. Instead, the shape and position of the receptor-binding region on a virus probably dictates receptor binding and subsequent uncoating events and has little or no influence on concealing the virus from the immune system. Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon.,Smith TJ, Chase ES, Schmidt TJ, Olson NH, Baker TS Nature. 1996 Sep 26;383(6598):350-4. PMID:8848050[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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