1hek: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px<br /><applet load="1hek" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hek, resolution 2.80Å" /> '''CRYSTAL STRUCTURE OF... |
No edit summary |
||
| (15 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==Crystal structure of equine infectious anaemia virus matrix antigen (EIAV MA)== | ||
The Gag polyprotein is key to the budding of retroviruses from host cells | <StructureSection load='1hek' size='340' side='right'caption='[[1hek]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1hek]] is a 2 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=1HEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HEK FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1hek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hek OCA], [https://pdbe.org/1hek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hek RCSB], [https://www.ebi.ac.uk/pdbsum/1hek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hek ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Gag polyprotein is key to the budding of retroviruses from host cells and is cleaved upon virion maturation, the N-terminal membrane-binding domain forming the matrix protein (MA). The 2.8-A resolution crystal structure of MA of equine infectious anemia virus (EIAV), a lentivirus, reveals that, despite showing no sequence similarity, more than half of the molecule can be superimposed on the MAs of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV). However, unlike the structures formed by HIV-1 and SIV MAs, the oligomerization state observed is not trimeric. We discuss the potential of this molecule for membrane binding in the light of conformational differences between EIAV MA and HIV or SIV MA. | |||
Structure of equine infectious anemia virus matrix protein.,Hatanaka H, Iourin O, Rao Z, Fry E, Kingsman A, Stuart DI J Virol. 2002 Feb;76(4):1876-83. PMID:11799182<ref>PMID:11799182</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1hek" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Gag polyprotein 3D structures|Gag polyprotein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Equine infectious anemia virus]] | [[Category: Equine infectious anemia virus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Fry | [[Category: Fry E]] | ||
[[Category: Hatanaka | [[Category: Hatanaka H]] | ||
[[Category: Iourin | [[Category: Iourin O]] | ||
[[Category: Kingsman | [[Category: Kingsman A]] | ||
[[Category: Rao | [[Category: Rao Z]] | ||
[[Category: Stuart | [[Category: Stuart DI]] | ||
Latest revision as of 10:25, 23 October 2024
Crystal structure of equine infectious anaemia virus matrix antigen (EIAV MA)Crystal structure of equine infectious anaemia virus matrix antigen (EIAV MA)
Structural highlights
FunctionGAG_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). Publication Abstract from PubMedThe Gag polyprotein is key to the budding of retroviruses from host cells and is cleaved upon virion maturation, the N-terminal membrane-binding domain forming the matrix protein (MA). The 2.8-A resolution crystal structure of MA of equine infectious anemia virus (EIAV), a lentivirus, reveals that, despite showing no sequence similarity, more than half of the molecule can be superimposed on the MAs of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV). However, unlike the structures formed by HIV-1 and SIV MAs, the oligomerization state observed is not trimeric. We discuss the potential of this molecule for membrane binding in the light of conformational differences between EIAV MA and HIV or SIV MA. Structure of equine infectious anemia virus matrix protein.,Hatanaka H, Iourin O, Rao Z, Fry E, Kingsman A, Stuart DI J Virol. 2002 Feb;76(4):1876-83. PMID:11799182[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||||