3d3t: Difference between revisions

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<StructureSection load='3d3t' size='340' side='right'caption='[[3d3t]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='3d3t' size='340' side='right'caption='[[3d3t]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3d3t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D3T FirstGlance]. <br>
<table><tr><td colspan='2'>[[3d3t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] and [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(Z2/CDC-Z34_ISOLATE) Human immunodeficiency virus type 1 (Z2/CDC-Z34 ISOLATE)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D3T FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag-pol ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1])</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]] 2.8&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] </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=3d3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d3t OCA], [https://pdbe.org/3d3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d3t RCSB], [https://www.ebi.ac.uk/pdbsum/3d3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d3t 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=3d3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d3t OCA], [https://pdbe.org/3d3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d3t RCSB], [https://www.ebi.ac.uk/pdbsum/3d3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d3t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/Q90VT5_9HIV1 Q90VT5_9HIV1]] Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation (By similarity).[SAAS:SAAS012344_004_047815]  Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity).[SAAS:SAAS012344_004_052592] [[https://www.uniprot.org/uniprot/GAG_HV1Z2 GAG_HV1Z2]] Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu.  Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.  Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers.  p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1 (By similarity).
[https://www.uniprot.org/uniprot/Q90VT5_9HIV1 Q90VT5_9HIV1] Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation (By similarity).[SAAS:SAAS012344_004_047815]  Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity).[SAAS:SAAS012344_004_052592]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[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=3d3t ConSurf].
</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=3d3t ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The effect of amino acid variability between human immunodeficiency virus type 1 (HIV-1) clades on structure and the emergence of resistance mutations in HIV-1 protease has become an area of significant interest in recent years. We determined the first crystal structure of the HIV-1 CRF01_AE protease in complex with the p1-p6 substrate to a resolution of 2.8 A. Hydrogen bonding between the flap hinge and the protease core regions shows significant structural rearrangements in CRF01_AE protease compared to the clade B protease structure.
Structural analysis of human immunodeficiency virus type 1 CRF01_AE protease in complex with the substrate p1-p6.,Bandaranayake RM, Prabu-Jeyabalan M, Kakizawa J, Sugiura W, Schiffer CA J Virol. 2008 Jul;82(13):6762-6. Epub 2008 Apr 23. PMID:18434392<ref>PMID:18434392</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3d3t" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Immunodeficiency virus protease 3D structures|Immunodeficiency virus protease 3D structures]]
*[[Immunodeficiency virus protease 3D structures|Immunodeficiency virus protease 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: HIV-1 retropepsin]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bandaranayake, R M]]
[[Category: Bandaranayake RM]]
[[Category: Kakizawa, J]]
[[Category: Kakizawa J]]
[[Category: Prabu-Jeyabalan, M]]
[[Category: Prabu-Jeyabalan M]]
[[Category: Schiffer, C A]]
[[Category: Schiffer CA]]
[[Category: Sugiura, W]]
[[Category: Sugiura W]]
[[Category: Aid]]
[[Category: Aspartyl protease]]
[[Category: Crf01_ae]]
[[Category: Hiv-1 protease]]
[[Category: Hydrolase]]
[[Category: Non-b clade]]
[[Category: P1-p6 substrate]]
Retrieved from "https://proteopedia.org/3d3t"