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[[Image:2r02.jpg|left|200px]]<br /><applet load="2r02" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2r02, resolution 2.60&Aring;" />
'''Crystal Structure of ALIX/AIP1 in complex with the HIV-1 YPLTSL Late Domain'''<br />


==Overview==
==Crystal Structure of ALIX/AIP1 in complex with the HIV-1 YPLTSL Late Domain==
Retrovirus budding requires short peptide motifs (late domains) located, within the viral Gag protein that function by recruiting cellular factors., The YPX(n)L late domains of HIV and other lentiviruses recruit the protein, ALIX (also known as AIP1), which also functions in vesicle formation at, the multivesicular body and in the abscission stage of cytokinesis. Here, we report the crystal structures of ALIX in complex with the YPX(n)L late, domains from HIV-1 and EIAV. The two distinct late domains bind at the, same site on the ALIX V domain but adopt different conformations that, allow them to make equivalent contacts. Binding studies and functional, assays verified the importance of key interface residues and revealed that, binding affinities are tuned by context-dependent effects. These results, reveal how YPX(n)L late domains recruit ALIX to facilitate virus budding, and how ALIX can bind YPX(n)L sequences with both n = 1 and n = 3.
<StructureSection load='2r02' size='340' side='right'caption='[[2r02]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[2r02]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/HIV-1_M:J_SE9173 HIV-1 M:J_SE9173] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R02 FirstGlance]. <br>
2R02 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2R02 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=2r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r02 OCA], [https://pdbe.org/2r02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r02 RCSB], [https://www.ebi.ac.uk/pdbsum/2r02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r02 ProSAT]</span></td></tr>
==Reference==
</table>
Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV., Zhai Q, Fisher RD, Chung HY, Myszka DG, Sundquist WI, Hill CP, Nat Struct Mol Biol. 2008 Jan;15(1):43-9. Epub 2007 Dec 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18066081 18066081]
== Function ==
[https://www.uniprot.org/uniprot/PDC6I_HUMAN PDC6I_HUMAN] Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Appears to be an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function implies the interaction with CHMP4B. May play a role in the regulation of both apoptosis and cell proliferation.<ref>PMID:14505569</ref> <ref>PMID:14505570</ref> <ref>PMID:14739459</ref> <ref>PMID:17853893</ref> <ref>PMID:17428861</ref> <ref>PMID:17556548</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r0/2r02_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2r02 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: HIV-1 M:J_SE9173]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Fisher, R.D.]]
[[Category: Fisher RD]]
[[Category: Hill, C.P.]]
[[Category: Hill CP]]
[[Category: Zhai, Q.]]
[[Category: Zhai Q]]
[[Category: aids]]
[[Category: apoptosis]]
[[Category: capsid protein]]
[[Category: coiled-coil]]
[[Category: cytoplasm]]
[[Category: host-virus interaction]]
[[Category: lipoprotein]]
[[Category: membrane]]
[[Category: metal-binding]]
[[Category: myristate]]
[[Category: nucleus]]
[[Category: peptide]]
[[Category: phosphorylation]]
[[Category: polymorphism]]
[[Category: protein transport]]
[[Category: rna-binding]]
[[Category: transport]]
[[Category: viral nucleoprotein]]
[[Category: virion]]
[[Category: zinc]]
[[Category: zinc-finger]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:13:19 2008''

Latest revision as of 12:19, 21 February 2024

Crystal Structure of ALIX/AIP1 in complex with the HIV-1 YPLTSL Late DomainCrystal Structure of ALIX/AIP1 in complex with the HIV-1 YPLTSL Late Domain

Structural highlights

2r02 is a 2 chain structure with sequence from HIV-1 M:J_SE9173 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PDC6I_HUMAN Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Appears to be an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function implies the interaction with CHMP4B. May play a role in the regulation of both apoptosis and cell proliferation.[1] [2] [3] [4] [5] [6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Strack B, Calistri A, Craig S, Popova E, Gottlinger HG. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell. 2003 Sep 19;114(6):689-99. PMID:14505569
  2. ↑ von Schwedler UK, Stuchell M, Muller B, Ward DM, Chung HY, Morita E, Wang HE, Davis T, He GP, Cimbora DM, Scott A, Krausslich HG, Kaplan J, Morham SG, Sundquist WI. The protein network of HIV budding. Cell. 2003 Sep 19;114(6):701-13. PMID:14505570
  3. ↑ Matsuo H, Chevallier J, Mayran N, Le Blanc I, Ferguson C, Faure J, Blanc NS, Matile S, Dubochet J, Sadoul R, Parton RG, Vilbois F, Gruenberg J. Role of LBPA and Alix in multivesicular liposome formation and endosome organization. Science. 2004 Jan 23;303(5657):531-4. PMID:14739459 doi:10.1126/science.1092425
  4. ↑ Morita E, Sandrin V, Chung HY, Morham SG, Gygi SP, Rodesch CK, Sundquist WI. Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO J. 2007 Oct 3;26(19):4215-27. Epub 2007 Sep 13. PMID:17853893 doi:10.1038/sj.emboj.7601850
  5. ↑ Usami Y, Popov S, Gottlinger HG. Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site. J Virol. 2007 Jun;81(12):6614-22. Epub 2007 Apr 11. PMID:17428861 doi:10.1128/JVI.00314-07
  6. ↑ Carlton JG, Martin-Serrano J. Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery. Science. 2007 Jun 29;316(5833):1908-12. Epub 2007 Jun 7. PMID:17556548 doi:10.1126/science.1143422

2r02, resolution 2.60Å

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