5c8c: Difference between revisions

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==Crystal structure of recombinant coxsackievirus A16 capsid==
==Crystal structure of recombinant coxsackievirus A16 capsid==
<StructureSection load='5c8c' size='340' side='right' caption='[[5c8c]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='5c8c' size='340' side='right'caption='[[5c8c]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5c8c]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C8C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C8C FirstGlance]. <br>
<table><tr><td colspan='2'>[[5c8c]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Coxsackievirus_A16_(strain_Tainan/5079/98) Coxsackievirus A16 (strain Tainan/5079/98)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C8C FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=STE:STEARIC+ACID'>STE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c4w|5c4w]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=STE:STEARIC+ACID'>STE</scene></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=5c8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c8c OCA], [http://pdbe.org/5c8c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c8c RCSB], [http://www.ebi.ac.uk/pdbsum/5c8c PDBsum]</span></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=5c8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c8c OCA], [https://pdbe.org/5c8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c8c RCSB], [https://www.ebi.ac.uk/pdbsum/5c8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c8c ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/I3W9E1_9ENTO I3W9E1_9ENTO]] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] 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).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047]
[https://www.uniprot.org/uniprot/POLG_CX16T POLG_CX16T] Protein VP1: Forms, together with VP2 and VP3, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Protein VP1 mainly forms the vertices of the capsid. VP1 interacts with host cell receptor to provide virion attachment to target cell. After binding to its receptor, the capsid undergoes conformational changes. VP1 N-terminus (that contains an amphipathic alpha-helix) is externalized, VP4 is released and together, they shape a virion-cell connecting channel and a pore in the host membrane through which RNase-protected transfer of the viral genome takes place. After genome has been released, the channel shrinks (By similarity).  Protein VP2: Forms, together with VP1 and VP3, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).  Protein VP3: Forms, together with VP1 and VP2, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).  Protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. VP4 is released, VP1 N-terminus is externalized, and together, they shape a virion-cell connecting channel and a pore in the host membrane through which RNase-protected transfer of the viral genome takes place. After genome has been released, the channel shrinks (By similarity).  Protein VP0: Protein VP0: VP0 precursor is a component of immature procapsids, which gives rise to VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).  Protease 2A: 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 off 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. It also inhibits endoplasmic reticulum-to-Golgi transport (By similarity).  Protease 3C: 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 cooperatively to the protease (By similarity).  RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
<div class="pdbe-citations 5c8c" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5c8c" style="background-color:#fffaf0;"></div>
==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Fry, E E]]
[[Category: Large Structures]]
[[Category: Gao, Q]]
[[Category: Fry EE]]
[[Category: Hu, Z]]
[[Category: Gao Q]]
[[Category: Li, X]]
[[Category: Hu Z]]
[[Category: Rao, Z]]
[[Category: Li X]]
[[Category: Ren, J]]
[[Category: Rao Z]]
[[Category: Shen, X]]
[[Category: Ren J]]
[[Category: Stuart, D I]]
[[Category: Shen X]]
[[Category: Wang, J]]
[[Category: Stuart DI]]
[[Category: Wang, X]]
[[Category: Wang J]]
[[Category: Yang, P]]
[[Category: Wang X]]
[[Category: Zhu, L]]
[[Category: Yang P]]
[[Category: Hand-foot-and-mouth disease]]
[[Category: Zhu L]]
[[Category: Icosahedral virus]]
[[Category: Immunogenicity]]
[[Category: Picornavirus]]
[[Category: Virus]]

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