6oqa - Revision history

OCA at 14:52, 13 March 2024

2024-03-13T14:52:46Z

←Older revision		Revision as of 14:52, 13 March 2024
Line 3:		Line 3:
	<StructureSection load='6oqa' size='340' side='right'caption='[[6oqa]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='6oqa' size='340' side='right'caption='[[6oqa]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6oqa]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OQA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6OQA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6oqa]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OQA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=60Z:(3R,4E,7E,10R,11S,12R,13S,16R,17R,24aS)-11,17-dihydroxy-10,12,16-trimethyl-3-[(2R)-1-phenylbutan-2-yl]-6,9,10,11,12,13,14,15,16,17,22,23,24,24a-tetradecahydro-3H-13,17-epoxypyrido[2,1-c][1,4]oxazacyclohenicosine-1,18,19(21H)-trione'>60Z</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 2.2Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CEP250, CEP2, CNAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=60Z:(3R,4E,7E,10R,11S,12R,13S,16R,17R,24aS)-11,17-dihydroxy-10,12,16-trimethyl-3-[(2R)-1-phenylbutan-2-yl]-6,9,10,11,12,13,14,15,16,17,22,23,24,24a-tetradecahydro-3H-13,17-epoxypyrido[2,1-c][1,4]oxazacyclohenicosine-1,18,19(21H)-trione'>60Z</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=6oqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oqa OCA], [https://pdbe.org/6oqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oqa RCSB], [https://www.ebi.ac.uk/pdbsum/6oqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oqa 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=6oqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oqa OCA], [~~http~~://pdbe.org/6oqa PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6oqa RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6oqa PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6oqa ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/CP250_HUMAN CP250_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FKB1A_HUMAN FKB1A_HUMAN]] Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:9233797</ref> <ref>PMID:16720724</ref> [[http://www.uniprot.org/uniprot/CP250_HUMAN CP250_HUMAN]] May be involved in ciliogenesis (PubMed:28005958). Probably plays an important role in centrosome cohesion during interphase.<ref>PMID:28005958</ref>	+	[https://www.uniprot.org/uniprot/FKB1A_HUMAN FKB1A_HUMAN] Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:9233797</ref> <ref>PMID:16720724</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The vast majority of intracellular protein targets are refractory toward small-molecule therapeutic engagement, and additional therapeutic modalities are needed to overcome this deficiency. Here, the identification and characterization of a natural product, WDB002, reveals a therapeutic modality that dramatically expands the currently accepted limits of druggability. WDB002, in complex with the FK506-binding protein (FKBP12), potently and selectively binds the human centrosomal protein 250 (CEP250), resulting in disruption of CEP250 function in cells. The recognition mode is unprecedented in that the targeted domain of CEP250 is a coiled coil and is topologically featureless, embodying both a structural motif and surface topology previously considered on the extreme limits of "undruggability" for an intracellular target. Structural studies reveal extensive protein-WDB002 and protein-protein contacts, with the latter being distinct from those seen in FKBP12 ternary complexes formed by FK506 and rapamycin. Outward-facing structural changes in a bound small molecule can thus reprogram FKBP12 to engage diverse, otherwise "undruggable" targets. The flat-targeting modality demonstrated here has the potential to expand the druggable target range of small-molecule therapeutics. As CEP250 was recently found to be an interaction partner with the Nsp13 protein of the SARS-CoV-2 virus that causes COVID-19 disease, it is possible that WDB002 or an analog may exert useful antiviral activity through its ability to form high-affinity ternary complexes containing CEP250 and FKBP12.	+
-		+
-	Genomic discovery of an evolutionarily programmed modality for small-molecule targeting of an intractable protein surface.,Shigdel UK, Lee SJ, Sowa ME, Bowman BR, Robison K, Zhou M, Pua KH, Stiles DT, Blodgett JAV, Udwary DW, Rajczewski AT, Mann AS, Mostafavi S, Hardy T, Arya S, Weng Z, Stewart M, Kenyon K, Morgenstern JP, Pan E, Gray DC, Pollock RM, Fry AM, Klausner RD, Townson SA, Verdine GL Proc Natl Acad Sci U S A. 2020 Jul 21;117(29):17195-17203. doi:, 10.1073/pnas.2006560117. Epub 2020 Jun 30. PMID:32606248<ref>PMID:32606248</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6oqa" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 29:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Peptidylprolyl isomerase]]~~	+	[[Category: Lee S-J]]
-	[[Category: Lee, S J]]	+	[[Category: Shigdel UK]]
-	[[Category: Shigdel~~, U K~~]]	+	[[Category: Townson SA]]
-	[[Category: Townson~~, S A~~]]	+	[[Category: Verdine GL]]
-	[[Category: Verdine~~, G L]]~~	+
-	~~[[Category: Cell cycle]]~~	+
-	~~[[Category: Cep250]]~~	+
-	~~[[Category: Fkbp12]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Natural product]]~~	+
-	~~[[Category: Ternary complex~~]]	+

OCA at 08:07, 11 November 2020

2020-11-11T08:07:37Z

←Older revision		Revision as of 08:07, 11 November 2020
Line 1:		Line 1:

	==Crystal structure of CEP250 bound to FKBP12 in the presence of FK506-like novel natural product==		==Crystal structure of CEP250 bound to FKBP12 in the presence of FK506-like novel natural product==
-	<StructureSection load='6oqa' size='340' side='right'caption='[[6oqa]]' scene=''>	+	<StructureSection load='6oqa' size='340' side='right'caption='[[6oqa]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OQA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OQA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6oqa]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OQA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OQA FirstGlance]. <br>
-	</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=6oqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oqa OCA], [http://pdbe.org/6oqa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oqa RCSB], [http://www.ebi.ac.uk/pdbsum/6oqa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oqa ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=60Z:(3R,4E,7E,10R,11S,12R,13S,16R,17R,24aS)-11,17-dihydroxy-10,12,16-trimethyl-3-[(2R)-1-phenylbutan-2-yl]-6,9,10,11,12,13,14,15,16,17,22,23,24,24a-tetradecahydro-3H-13,17-epoxypyrido[2,1-c][1,4]oxazacyclohenicosine-1,18,19(21H)-trione'>60Z</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CEP250, CEP2, CNAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=6oqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oqa OCA], [http://pdbe.org/6oqa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oqa RCSB], [http://www.ebi.ac.uk/pdbsum/6oqa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oqa ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CP250_HUMAN CP250_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FKB1A_HUMAN FKB1A_HUMAN]] Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:9233797</ref> <ref>PMID:16720724</ref> [[http://www.uniprot.org/uniprot/CP250_HUMAN CP250_HUMAN]] May be involved in ciliogenesis (PubMed:28005958). Probably plays an important role in centrosome cohesion during interphase.<ref>PMID:28005958</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The vast majority of intracellular protein targets are refractory toward small-molecule therapeutic engagement, and additional therapeutic modalities are needed to overcome this deficiency. Here, the identification and characterization of a natural product, WDB002, reveals a therapeutic modality that dramatically expands the currently accepted limits of druggability. WDB002, in complex with the FK506-binding protein (FKBP12), potently and selectively binds the human centrosomal protein 250 (CEP250), resulting in disruption of CEP250 function in cells. The recognition mode is unprecedented in that the targeted domain of CEP250 is a coiled coil and is topologically featureless, embodying both a structural motif and surface topology previously considered on the extreme limits of "undruggability" for an intracellular target. Structural studies reveal extensive protein-WDB002 and protein-protein contacts, with the latter being distinct from those seen in FKBP12 ternary complexes formed by FK506 and rapamycin. Outward-facing structural changes in a bound small molecule can thus reprogram FKBP12 to engage diverse, otherwise "undruggable" targets. The flat-targeting modality demonstrated here has the potential to expand the druggable target range of small-molecule therapeutics. As CEP250 was recently found to be an interaction partner with the Nsp13 protein of the SARS-CoV-2 virus that causes COVID-19 disease, it is possible that WDB002 or an analog may exert useful antiviral activity through its ability to form high-affinity ternary complexes containing CEP250 and FKBP12.
		+
		+	Genomic discovery of an evolutionarily programmed modality for small-molecule targeting of an intractable protein surface.,Shigdel UK, Lee SJ, Sowa ME, Bowman BR, Robison K, Zhou M, Pua KH, Stiles DT, Blodgett JAV, Udwary DW, Rajczewski AT, Mann AS, Mostafavi S, Hardy T, Arya S, Weng Z, Stewart M, Kenyon K, Morgenstern JP, Pan E, Gray DC, Pollock RM, Fry AM, Klausner RD, Townson SA, Verdine GL Proc Natl Acad Sci U S A. 2020 Jul 21;117(29):17195-17203. doi:, 10.1073/pnas.2006560117. Epub 2020 Jun 30. PMID:32606248<ref>PMID:32606248</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6oqa" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[FKBP 3D structures\|FKBP 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Lee S-J]]	+	[[Category: Peptidylprolyl isomerase]]
-	[[Category: Shigdel UK]]	+	[[Category: Lee, S J]]
-	[[Category: Townson SA]]	+	[[Category: Shigdel, U K]]
-	[[Category: Verdine GL]]	+	[[Category: Townson, S A]]
		+	[[Category: Verdine, G L]]
		+	[[Category: Cell cycle]]
		+	[[Category: Cep250]]
		+	[[Category: Fkbp12]]
		+	[[Category: Isomerase]]
		+	[[Category: Natural product]]
		+	[[Category: Ternary complex]]

OCA at 06:42, 29 April 2020

2020-04-29T06:42:02Z

←Older revision		Revision as of 06:42, 29 April 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 6oqa is ON HOLD until Paper Publication~~	+	==Crystal structure of CEP250 bound to FKBP12 in the presence of FK506-like novel natural product==
-		+	<StructureSection load='6oqa' size='340' side='right'caption='[[6oqa]]' scene=''>
-	~~Authors: Lee, S.-J., Shigdel, U.K., Townson, S.A., Verdine, G.L.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OQA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OQA FirstGlance]. <br>
-	~~Description:~~ Crystal structure of CEP250 bound to FKBP12 in the presence of FK506-like novel natural product	+	</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=6oqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oqa OCA], [http://pdbe.org/6oqa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oqa RCSB], [http://www.ebi.ac.uk/pdbsum/6oqa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oqa ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[[~~Category~~: ~~Shigdel~~, U.K]]	+	__TOC__
-	[[Category: ~~Townson, S.A~~]]	+	</StructureSection>
-	[[Category: Lee, S.-J]]	+	[[Category: Large Structures]]
-	[[Category: Verdine~~, G.L~~]]	+	[[Category: Lee S-J]]
		+	[[Category: Shigdel UK]]
		+	[[Category: Townson SA]]
		+	[[Category: Verdine GL]]

OCA at 03:59, 22 May 2019

2019-05-22T03:59:52Z

←Older revision		Revision as of 03:59, 22 May 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6oqa is ON HOLD	+	The entry 6oqa is ON HOLD until Paper Publication

	Authors: Lee, S.-J., Shigdel, U.K., Townson, S.A., Verdine, G.L.		Authors: Lee, S.-J., Shigdel, U.K., Townson, S.A., Verdine, G.L.
Line 7:		Line 7:
	Description: Crystal structure of CEP250 bound to FKBP12 in the presence of FK506-like novel natural product		Description: Crystal structure of CEP250 bound to FKBP12 in the presence of FK506-like novel natural product
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Townson, S.A]]
-	[[Category: Verdine, G.L]]
	[[Category: Shigdel, U.K]]		[[Category: Shigdel, U.K]]
		+	[[Category: Townson, S.A]]
	[[Category: Lee, S.-J]]		[[Category: Lee, S.-J]]
		+	[[Category: Verdine, G.L]]

OCA: Protected "6oqa" [edit=sysop:move=sysop]

2019-05-01T07:19:47Z

Protected "6oqa" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:19, 1 May 2019

OCA: New page: '''Unreleased structure''' The entry 6oqa is ON HOLD Authors: Lee, S.-J., Shigdel, U.K., Townson, S.A., Verdine, G.L. Description: Crystal structure of CEP250 bound to FKBP12 in the pr...

2019-05-01T07:19:46Z

New page: '''Unreleased structure''' The entry 6oqa is ON HOLD Authors: Lee, S.-J., Shigdel, U.K., Townson, S.A., Verdine, G.L. Description: Crystal structure of CEP250 bound to FKBP12 in the pr...

New page

'''Unreleased structure'''

The entry 6oqa is ON HOLD

Authors: Lee, S.-J., Shigdel, U.K., Townson, S.A., Verdine, G.L.

Description: Crystal structure of CEP250 bound to FKBP12 in the presence of FK506-like novel natural product
[[Category: Unreleased Structures]]
[[Category: Townson, S.A]]
[[Category: Verdine, G.L]]
[[Category: Shigdel, U.K]]
[[Category: Lee, S.-J]]