1eia: Difference between revisions

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 <StructureSection load='1eia' size='340' side='right'caption='[[1eia]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1eia]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eiav Eiav]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1EIA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1eia]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EIA FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GAG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11665 EIAV])</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]] 2.7&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1eia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eia OCA], [http://pdbe.org/1eia PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eia RCSB], [http://www.ebi.ac.uk/pdbsum/1eia PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1eia ProSAT]</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=1eia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eia OCA], [https://pdbe.org/1eia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eia RCSB], [https://www.ebi.ac.uk/pdbsum/1eia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eia ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GAG_EIAVY GAG_EIAVY]] Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane (By similarity).  Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).  Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).  p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1 (By similarity).
+[https://www.uniprot.org/uniprot/GAG_EIAVY GAG_EIAVY] Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane (By similarity).  Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).  Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).  p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1 (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eia ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Two crystal forms of recombinant p26 capsid protein (CA) from the equine infectious anemia virus (EIAV) have in common an antiparallel four-helix bundle dimer interface between N-terminal domains (NTDs). The dimer interface provides a lenient scaffold to accommodate the wide sequence variation in these helices within lentivirus CA. Pairs of dimers weakly associate to form exact or approximate D2 symmetry tetramers. In one of the two crystal forms, the tetramers are linked via dimerization of C-terminal domains (CTDs). We propose that the observed NTD and CTD homodimer interactions are involved in the assembly of the lentivirus capsid. The NTD homodimer shape readily suggests a model for the mature capsid core, based on hexagonal packing with dimensions and surface topology resembling described EIAV capsid cores. Combining available data for human immunodeficiency virus and EIAV CA, we also propose an assembly pathway for maturation of the lentivirus capsid core following proteolytic cleavage of the gag polyprotein precursor.
-Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26.,Jin Z, Jin L, Peterson DL, Lawson CL J Mol Biol. 1999 Feb 12;286(1):83-93. PMID:9931251<ref>PMID:9931251</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1eia" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Eiav]]
+[[Category: Equine infectious anemia virus]]
 [[Category: Large Structures]]
-[[Category: Jin, L]]
+[[Category: Jin L]]
-[[Category: Jin, Z]]
+[[Category: Jin Z]]
-[[Category: Lawson, C L]]
+[[Category: Lawson CL]]
-[[Category: Peterson, D L]]
+[[Category: Peterson DL]]
-[[Category: Hiv]]
-[[Category: Lentivirus]]
-[[Category: Viral capsid]]
-[[Category: Viral protein]]