5ea3 - Revision history

OCA at 06:18, 5 July 2023

2023-07-05T06:18:39Z

← Older revision		Revision as of 06:18, 5 July 2023
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	<StructureSection load='5ea3' size='340' side='right'caption='[[5ea3]], [[Resolution\|resolution]] 2.75Å' scene=''>		<StructureSection load='5ea3' size='340' side='right'caption='[[5ea3]], [[Resolution\|resolution]] 2.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5ea3]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Hrsva Hrsva~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EA3 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5EA3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5ea3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_respiratory_syncytial_virus_A2 Human respiratory syncytial virus A2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EA3 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5NK:2-[[2-[[1-(2-AZANYLETHYL)PIPERIDIN-4-YL]AMINO]-4-METHYL-BENZIMIDAZOL-1-YL]METHYL]-6-METHYL-PYRIDIN-3-OL'>5NK</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.75Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mmu\|4mmu]], [[5ea4\|5ea4]], [[5ea5\|5ea5]], [[5ea7\|5ea7]], [[5ea6\|5ea6]], [[5ea8\|5ea8]]~~</td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5NK:2-[[2-[[1-(2-AZANYLETHYL)PIPERIDIN-4-YL]AMINO]-4-METHYL-BENZIMIDAZOL-1-YL]METHYL]-6-METHYL-PYRIDIN-3-OL'>5NK</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5ea3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ea3 OCA], [~~http~~://pdbe.org/5ea3 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5ea3 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5ea3 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5ea3 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=5ea3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ea3 OCA], [https://pdbe.org/5ea3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ea3 RCSB], [https://www.ebi.ac.uk/pdbsum/5ea3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ea3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/FUS_HRSVA FUS_HRSVA]] Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (protein F) interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between host cell and virion membranes. Notably, RSV fusion protein is able to interact directly with heparan sulfate and therefore actively participates in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. Later in infection, proteins F expressed at the plasma membrane of infected cells mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. The fusion protein is also able to trigger p53-dependent apoptosis.<ref>PMID:12663767</ref> <ref>PMID:18216092</ref>		[https://www.uniprot.org/uniprot/FUS_HRSVA FUS_HRSVA] Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (protein F) interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between host cell and virion membranes. Notably, RSV fusion protein is able to interact directly with heparan sulfate and therefore actively participates in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. Later in infection, proteins F expressed at the plasma membrane of infected cells mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. The fusion protein is also able to trigger p53-dependent apoptosis.<ref>PMID:12663767</ref> <ref>PMID:18216092</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Hrsva~~]]		[[Category: Human respiratory syncytial virus A2]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Arnoult, E]]		[[Category: Arnoult E]]
	[[Category: Battles~~, M B~~]]		[[Category: Battles MB]]
	[[Category: Langedijk~~, J P~~]]		[[Category: Langedijk JP]]
	[[Category: McLellan~~, J S~~]]		[[Category: McLellan JS]]
	[[Category: Roymans, D]]		[[Category: Roymans D]]
	~~[[Category: Cell invasion-inhibitor complex]]~~
	~~[[Category: Class i viral fusion protein]]~~
	~~[[Category: Fusion]]~~
	~~[[Category: Fusion inhibitor]]~~
	~~[[Category: Prefusion]]~~
	~~[[Category: Respiratory syncytial virus]]~~
	~~[[Category: Viral protein~~]]

OCA at 06:49, 22 April 2020

2020-04-22T06:49:52Z

← Older revision		Revision as of 06:49, 22 April 2020
Line 1:		Line 1:

	==Crystal Structure of Inhibitor JNJ-2408068 in Complex with Prefusion RSV F Glycoprotein==		==Crystal Structure of Inhibitor JNJ-2408068 in Complex with Prefusion RSV F Glycoprotein==
	<StructureSection load='5ea3' size='340' side='right' caption='[[5ea3]], [[Resolution\|resolution]] 2.75Å' scene=''>		<StructureSection load='5ea3' size='340' side='right'caption='[[5ea3]], [[Resolution\|resolution]] 2.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5ea3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EA3 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca.weizmann.ac~~.~~il/oca-docs~~/fgij/fg.htm?mol=5EA3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5ea3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrsva Hrsva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EA3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EA3 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5NK:2-[[2-[[1-(2-AZANYLETHYL)PIPERIDIN-4-YL]AMINO]-4-METHYL-BENZIMIDAZOL-1-YL]METHYL]-6-METHYL-PYRIDIN-3-OL'>5NK</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5NK:2-[[2-[[1-(2-AZANYLETHYL)PIPERIDIN-4-YL]AMINO]-4-METHYL-BENZIMIDAZOL-1-YL]METHYL]-6-METHYL-PYRIDIN-3-OL'>5NK</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mmu\|4mmu]], [[5ea4\|5ea4]], [[5ea5\|5ea5]], [[5ea7\|5ea7]], [[5ea6\|5ea6]], [[5ea8\|5ea8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mmu\|4mmu]], [[5ea4\|5ea4]], [[5ea5\|5ea5]], [[5ea7\|5ea7]], [[5ea6\|5ea6]], [[5ea8\|5ea8]]</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=5ea3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ea3 OCA], [http://pdbe.org/5ea3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ea3 RCSB], [http://www.ebi.ac.uk/pdbsum/5ea3 PDBsum]</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=5ea3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ea3 OCA], [http://pdbe.org/5ea3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ea3 RCSB], [http://www.ebi.ac.uk/pdbsum/5ea3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ea3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 22:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Hrsva]]
			[[Category: Large Structures]]
	[[Category: Arnoult, E]]		[[Category: Arnoult, E]]
	[[Category: Battles, M B]]		[[Category: Battles, M B]]

OCA at 06:24, 23 December 2015

2015-12-23T06:24:57Z

← Older revision		Revision as of 06:24, 23 December 2015
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FUS_HRSVA FUS_HRSVA]] Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (protein F) interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between host cell and virion membranes. Notably, RSV fusion protein is able to interact directly with heparan sulfate and therefore actively participates in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. Later in infection, proteins F expressed at the plasma membrane of infected cells mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. The fusion protein is also able to trigger p53-dependent apoptosis.<ref>PMID:12663767</ref> <ref>PMID:18216092</ref>		[[http://www.uniprot.org/uniprot/FUS_HRSVA FUS_HRSVA]] Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (protein F) interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between host cell and virion membranes. Notably, RSV fusion protein is able to interact directly with heparan sulfate and therefore actively participates in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. Later in infection, proteins F expressed at the plasma membrane of infected cells mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. The fusion protein is also able to trigger p53-dependent apoptosis.<ref>PMID:12663767</ref> <ref>PMID:18216092</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Respiratory syncytial virus (RSV) is a leading cause of pneumonia and bronchiolitis in young children and the elderly. Therapeutic small molecules have been developed that bind the RSV F glycoprotein and inhibit membrane fusion, yet their binding sites and molecular mechanisms of action remain largely unknown. Here we show that these inhibitors bind to a three-fold-symmetric pocket within the central cavity of the metastable prefusion conformation of RSV F. Inhibitor binding stabilizes this conformation by tethering two regions that must undergo a structural rearrangement to facilitate membrane fusion. Inhibitor-escape mutations occur in residues that directly contact the inhibitors or are involved in the conformational rearrangements required to accommodate inhibitor binding. Resistant viruses do not propagate as well as wild-type RSV in vitro, indicating a fitness cost for inhibitor escape. Collectively, these findings provide new insight into class I viral fusion proteins and should facilitate development of optimal RSV fusion inhibitors.

			Molecular mechanism of respiratory syncytial virus fusion inhibitors.,Battles MB, Langedijk JP, Furmanova-Hollenstein P, Chaiwatpongsakorn S, Costello HM, Kwanten L, Vranckx L, Vink P, Jaensch S, Jonckers TH, Koul A, Arnoult E, Peeples ME, Roymans D, McLellan JS Nat Chem Biol. 2015 Dec 7. doi: 10.1038/nchembio.1982. PMID:26641933<ref>PMID:26641933</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 5ea3" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:50, 9 December 2015

2015-12-09T13:50:08Z

← Older revision		Revision as of 13:50, 9 December 2015
Line 1:		Line 1:
	'''~~Unreleased structure~~'''		==Crystal Structure of Inhibitor JNJ-2408068 in Complex with Prefusion RSV F Glycoprotein==
			<StructureSection load='5ea3' size='340' side='right' caption='[[5ea3]], [[Resolution\|resolution]] 2.75Å' scene=''>
	~~The entry~~ 5ea3 is ~~ON HOLD~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[5ea3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EA3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EA3 FirstGlance]. <br>
	~~Authors~~: ~~Battles~~, M.B., ~~McLellan, J~~.S., ~~Arnoult~~, E., ~~Langedijk, J~~.P.~~, Roymans, D~~.		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5NK:2-[[2-[[1-(2-AZANYLETHYL)PIPERIDIN-4-YL]AMINO]-4-METHYL-BENZIMIDAZOL-1-YL]METHYL]-6-METHYL-PYRIDIN-3-OL'>5NK</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mmu\|4mmu]], [[5ea4\|5ea4]], [[5ea5\|5ea5]], [[5ea7\|5ea7]], [[5ea6\|5ea6]], [[5ea8\|5ea8]]</td></tr>
	~~Description~~: ~~Crystal Structure~~ of ~~Inhibitor JNJ~~-~~2408068~~ in ~~Complex~~ with ~~Prefusion~~ RSV F ~~Glycoprotein~~		<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=5ea3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ea3 OCA], [http://pdbe.org/5ea3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ea3 RCSB], [http://www.ebi.ac.uk/pdbsum/5ea3 PDBsum]</span></td></tr>
	[[Category: ~~Unreleased Structures~~]]		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/FUS_HRSVA FUS_HRSVA]] Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (protein F) interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between host cell and virion membranes. Notably, RSV fusion protein is able to interact directly with heparan sulfate and therefore actively participates in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. Later in infection, proteins F expressed at the plasma membrane of infected cells mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. The fusion protein is also able to trigger p53-dependent apoptosis.<ref>PMID:12663767</ref> <ref>PMID:18216092</ref>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Arnoult, E]]
			[[Category: Battles, M B]]
			[[Category: Langedijk, J P]]
			[[Category: McLellan, J S]]
	[[Category: Roymans, D]]		[[Category: Roymans, D]]
	[[Category: ~~Mclellan, J.S~~]]		[[Category: Cell invasion-inhibitor complex]]
	[[Category: ~~Battles, M.B~~]]		[[Category: Class i viral fusion protein]]
	[[Category: ~~Arnoult, E~~]]		[[Category: Fusion]]
	[[Category: ~~Langedijk, J.P~~]]		[[Category: Fusion inhibitor]]
			[[Category: Prefusion]]
			[[Category: Respiratory syncytial virus]]
			[[Category: Viral protein]]

OCA at 02:33, 1 December 2015

2015-12-01T02:33:58Z

← Older revision		Revision as of 02:33, 1 December 2015
Line 5:		Line 5:
	Authors: Battles, M.B., McLellan, J.S., Arnoult, E., Langedijk, J.P., Roymans, D.		Authors: Battles, M.B., McLellan, J.S., Arnoult, E., Langedijk, J.P., Roymans, D.

	Description: Crystal Structure of Inhibitor JNJ-2408068 In Complex with Prefusion RSV F Glycoprotein		Description: Crystal Structure of Inhibitor JNJ-2408068 in Complex with Prefusion RSV F Glycoprotein
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Roymans, D]]		[[Category: Roymans, D]]

OCA: Protected "5ea3" [edit=sysop:move=sysop]

2015-10-22T04:35:20Z

Protected "5ea3" [edit=sysop:move=sysop]

← Older revision	Revision as of 04:35, 22 October 2015
(No difference)

OCA: New page: '''Unreleased structure''' The entry 5ea3 is ON HOLD Authors: Battles, M.B., McLellan, J.S., Arnoult, E., Langedijk, J.P., Roymans, D. Description: Crystal Structure of Inhibitor JNJ-2...

2015-10-22T04:35:19Z

New page: '''Unreleased structure''' The entry 5ea3 is ON HOLD Authors: Battles, M.B., McLellan, J.S., Arnoult, E., Langedijk, J.P., Roymans, D. Description: Crystal Structure of Inhibitor JNJ-2...

New page

'''Unreleased structure'''

The entry 5ea3 is ON HOLD

Authors: Battles, M.B., McLellan, J.S., Arnoult, E., Langedijk, J.P., Roymans, D.

Description: Crystal Structure of Inhibitor JNJ-2408068 In Complex with Prefusion RSV F Glycoprotein
[[Category: Unreleased Structures]]
[[Category: Roymans, D]]
[[Category: Mclellan, J.S]]
[[Category: Battles, M.B]]
[[Category: Arnoult, E]]
[[Category: Langedijk, J.P]]