5yoj - Revision history

OCA at 10:24, 27 March 2024

OCA — Wed, 27 Mar 2024 10:24:29 GMT

←Older revision		Revision as of 10:24, 27 March 2024
Line 3:		Line 3:
	<StructureSection load='5yoj' size='340' side='right'caption='[[5yoj]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='5yoj' size='340' side='right'caption='[[5yoj]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5yoj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YOJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5YOJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5yoj]] is a 2 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=5YOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YOJ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8Z0:(4R)-N-[(2,6-dimethylphenyl)methyl]-3-[(2S,3S)-3-[[(2S)-2-[(7-methoxy-1-benzofuran-2-yl)carbonylamino]-2-[(3R)-oxolan-3-yl]ethanoyl]amino]-2-oxidanyl-4-phenyl-butanoyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxamide'>8Z0</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.5Å</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] </span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8Z0:(4R)-N-[(2,6-dimethylphenyl)methyl]-3-[(2S,3S)-3-[[(2S)-2-[(7-methoxy-1-benzofuran-2-yl)carbonylamino]-2-[(3R)-oxolan-3+-yl]ethanoyl]amino]-2-oxidanyl-4-phenyl-butanoyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxamide'>8Z0</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5yoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yoj OCA], [~~http~~://pdbe.org/5yoj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5yoj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5yoj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5yoj 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=5yoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yoj OCA], [https://pdbe.org/5yoj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yoj RCSB], [https://www.ebi.ac.uk/pdbsum/5yoj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yoj ProSAT]</span></td></tr>
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[https://www.uniprot.org/uniprot/POL_HV1B1 POL_HV1B1] 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).<ref>PMID:9658129</ref> Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to play a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. It binds in the cytoplasm the human BAF protein which prevent autointegration of the viral genome, and might be included in virions at the ration of zero to 3 BAF dimer per virion. The myristoylation signal and the NLS thus exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu (By similarity).<ref>PMID:9658129</ref> Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (By similarity).<ref>PMID:9658129</ref> 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).<ref>PMID:9658129</ref> The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles (By similarity).<ref>PMID:9658129</ref> Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).<ref>PMID:9658129</ref> Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity).<ref>PMID:9658129</ref>
-	~~The emergence of drug~~-~~resistant HIV from a widespread antiviral chemotherapy targeting HIV protease~~ in the ~~past decades is unavoidable~~ and ~~provides a challenge~~ to ~~develop alternative inhibitors~~. ~~We synthesized~~ a ~~series~~ of ~~allophenylnorstatine~~-~~based peptidomimetics with various P3, P2~~, and ~~P2 moieties~~. The ~~derivatives with P2 tetrahydrofuranylglycine (Thfg) were found to~~ be ~~potent against wild type HIV~~-~~1 protease and~~ the virus, ~~leading to a highly potent compound 21f (KNI~~-~~1657~~) ~~against lopinavir~~/~~ritonavir~~- ~~or darunavir~~-~~resistant strains~~. Co-~~crystal structures~~ of ~~21f~~ and the ~~wild~~-~~type protease revealed numerous key hydrogen bonding interactions~~ with ~~Thfg~~. ~~These results suggest~~ that the ~~strategy~~ to ~~design allophenylnorstatine~~-~~based peptidomimetics combined with Thfg residue would be promising for generating candidates~~ to ~~overcome multidrug resistance~~.	+
-		+
-	~~Identification~~ of ~~Highly Potent Human Immunodeficiency Virus Type~~-~~1 Protease Inhibitors against Lopinavir and Darunavir Resistant Viruses from Allophenylnorstatine~~-~~Based Peptidomimetics with P2 Tetrahydrofuranylglycine~~.~~,Hidaka K, Kimura T, Sankaranarayanan~~ R, ~~Wang J, McDaniel KF, Kempf DJ, Kameoka M, Adachi M, Kuroki~~ R, ~~Nguyen JT~~, ~~Hayashi Y, Kiso Y J Med Chem~~. ~~2018 Jun 28;61~~(12)~~:5138~~-~~5153~~. ~~doi: 10~~.~~1021/acs~~.~~jmedchem~~.~~7b01709~~. ~~Epub~~, ~~2018 Jun 11~~. ~~PMID:29852069~~<ref>PMID:~~29852069~~</ref>	+
-		+
-	~~From MEDLINE®/PubMed®~~, a ~~database~~ of the U.S. ~~National Library~~ of ~~Medicine~~.~~<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe~~-~~citations 5yoj" style="background~~-~~color:#fffaf0;"~~></~~div~~>	+

	==See Also==		==See Also==
Line 24:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~HIV-~~1 ~~retropepsin~~]]	+	[[Category: Human immunodeficiency virus 1]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Adachi, M]]	+	[[Category: Adachi M]]
-	[[Category: Hidaka, K]]	+	[[Category: Hidaka K]]
-	[[Category: Kiso, Y]]	+	[[Category: Kiso Y]]
-	[[Category: Kuroki, R]]	+	[[Category: Kuroki R]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Inhibitor~~]]	+

OCA at 09:23, 21 October 2020

OCA — Wed, 21 Oct 2020 09:23:54 GMT

←Older revision		Revision as of 09:23, 21 October 2020
Line 1:		Line 1:

	==Structure of A17 HIV-1 Protease in Complex with Inhibitor KNI-1657==		==Structure of A17 HIV-1 Protease in Complex with Inhibitor KNI-1657==
-	<StructureSection load='5yoj' size='340' side='right' caption='[[5yoj]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='5yoj' size='340' side='right'caption='[[5yoj]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5yoj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YOJ OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5YOJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5yoj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YOJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YOJ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8Z0:(4R)-N-[(2,6-dimethylphenyl)methyl]-3-[(2S,3S)-3-[[(2S)-2-[(7-methoxy-1-benzofuran-2-yl)carbonylamino]-2-[(3R)-oxolan-3-yl]ethanoyl]amino]-2-oxidanyl-4-phenyl-butanoyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxamide'>8Z0</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8Z0:(4R)-N-[(2,6-dimethylphenyl)methyl]-3-[(2S,3S)-3-[[(2S)-2-[(7-methoxy-1-benzofuran-2-yl)carbonylamino]-2-[(3R)-oxolan-3-yl]ethanoyl]amino]-2-oxidanyl-4-phenyl-butanoyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxamide'>8Z0</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://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'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5yoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yoj OCA], [http://pdbe.org/5yoj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yoj RCSB], [http://www.ebi.ac.uk/pdbsum/5yoj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yoj ProSAT]</span></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=5yoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yoj OCA], [http://pdbe.org/5yoj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yoj RCSB], [http://www.ebi.ac.uk/pdbsum/5yoj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yoj ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 17:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 5yoj" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5yoj" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Immunodeficiency virus protease 3D structures\|Immunodeficiency virus protease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 22:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: HIV-1 retropepsin]]		[[Category: HIV-1 retropepsin]]
		+	[[Category: Large Structures]]
	[[Category: Adachi, M]]		[[Category: Adachi, M]]
	[[Category: Hidaka, K]]		[[Category: Hidaka, K]]

OCA at 05:40, 11 July 2018

OCA — Wed, 11 Jul 2018 05:40:00 GMT

←Older revision		Revision as of 05:40, 11 July 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5yoj is ~~ON HOLD until Paper~~ Publication	+	==Structure of A17 HIV-1 Protease in Complex with Inhibitor KNI-1657==
		+	<StructureSection load='5yoj' size='340' side='right' caption='[[5yoj]], [[Resolution\|resolution]] 1.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5yoj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YOJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YOJ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8Z0:(4R)-N-[(2,6-dimethylphenyl)methyl]-3-[(2S,3S)-3-[[(2S)-2-[(7-methoxy-1-benzofuran-2-yl)carbonylamino]-2-[(3R)-oxolan-3-yl]ethanoyl]amino]-2-oxidanyl-4-phenyl-butanoyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxamide'>8Z0</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5yoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yoj OCA], [http://pdbe.org/5yoj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yoj RCSB], [http://www.ebi.ac.uk/pdbsum/5yoj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yoj ProSAT]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The emergence of drug-resistant HIV from a widespread antiviral chemotherapy targeting HIV protease in the past decades is unavoidable and provides a challenge to develop alternative inhibitors. We synthesized a series of allophenylnorstatine-based peptidomimetics with various P3, P2, and P2 moieties. The derivatives with P2 tetrahydrofuranylglycine (Thfg) were found to be potent against wild type HIV-1 protease and the virus, leading to a highly potent compound 21f (KNI-1657) against lopinavir/ritonavir- or darunavir-resistant strains. Co-crystal structures of 21f and the wild-type protease revealed numerous key hydrogen bonding interactions with Thfg. These results suggest that the strategy to design allophenylnorstatine-based peptidomimetics combined with Thfg residue would be promising for generating candidates to overcome multidrug resistance.

-	~~Authors: Adachi, M~~., Hidaka, K., ~~Kuroki~~, R., ~~Kiso~~, Y.	+	Identification of Highly Potent Human Immunodeficiency Virus Type-1 Protease Inhibitors against Lopinavir and Darunavir Resistant Viruses from Allophenylnorstatine-Based Peptidomimetics with P2 Tetrahydrofuranylglycine.,Hidaka K, Kimura T, Sankaranarayanan R, Wang J, McDaniel KF, Kempf DJ, Kameoka M, Adachi M, Kuroki R, Nguyen JT, Hayashi Y, Kiso Y J Med Chem. 2018 Jun 28;61(12):5138-5153. doi: 10.1021/acs.jmedchem.7b01709. Epub, 2018 Jun 11. PMID:29852069<ref>PMID:29852069</ref>

-	~~Description: Structure~~ of ~~A17~~ HIV-1 ~~Protease in Complex with Inhibitor KNI-1657~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5yoj" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: HIV-1 retropepsin]]
		+	[[Category: Adachi, M]]
		+	[[Category: Hidaka, K]]
	[[Category: Kiso, Y]]		[[Category: Kiso, Y]]
	[[Category: Kuroki, R]]		[[Category: Kuroki, R]]
-	[[Category: ~~Hidaka, K~~]]	+	[[Category: Hydrolase]]
-	[[Category: ~~Adachi, M~~]]	+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: Inhibitor]]

OCA at 05:55, 6 December 2017

OCA — Wed, 06 Dec 2017 05:55:45 GMT

←Older revision		Revision as of 05:55, 6 December 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5yoj is ON HOLD	+	The entry 5yoj is ON HOLD until Paper Publication

	Authors: Adachi, M., Hidaka, K., Kuroki, R., Kiso, Y.		Authors: Adachi, M., Hidaka, K., Kuroki, R., Kiso, Y.

OCA: Protected "5yoj" [edit=sysop:move=sysop]

OCA — Wed, 08 Nov 2017 06:26:56 GMT

Protected "5yoj" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:26, 8 November 2017

OCA: New page: '''Unreleased structure''' The entry 5yoj is ON HOLD Authors: Adachi, M., Hidaka, K., Kuroki, R., Kiso, Y. Description: Structure of A17 HIV-1 Protease in Complex with Inhibitor KNI-16...

OCA — Wed, 08 Nov 2017 06:26:55 GMT

New page: '''Unreleased structure''' The entry 5yoj is ON HOLD Authors: Adachi, M., Hidaka, K., Kuroki, R., Kiso, Y. Description: Structure of A17 HIV-1 Protease in Complex with Inhibitor KNI-16...

New page

'''Unreleased structure'''

The entry 5yoj is ON HOLD

Authors: Adachi, M., Hidaka, K., Kuroki, R., Kiso, Y.

Description: Structure of A17 HIV-1 Protease in Complex with Inhibitor KNI-1657
[[Category: Unreleased Structures]]
[[Category: Kiso, Y]]
[[Category: Kuroki, R]]
[[Category: Hidaka, K]]
[[Category: Adachi, M]]