4ouh - Revision history

OCA at 12:42, 1 March 2024

OCA — Fri, 01 Mar 2024 12:42:01 GMT

←Older revision		Revision as of 12:42, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ouh]] is a 4 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=4OUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OUH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ouh]] is a 4 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=4OUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OUH FirstGlance]. <br>
-	</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=4ouh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ouh OCA], [https://pdbe.org/4ouh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ouh RCSB], [https://www.ebi.ac.uk/pdbsum/4ouh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ouh ProSAT]</span></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]] 2Å</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=4ouh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ouh OCA], [https://pdbe.org/4ouh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ouh RCSB], [https://www.ebi.ac.uk/pdbsum/4ouh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ouh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/PSMF1_HUMAN PSMF1_HUMAN] Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.<ref>PMID:10764772</ref>		[https://www.uniprot.org/uniprot/PSMF1_HUMAN PSMF1_HUMAN] Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.<ref>PMID:10764772</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Fbxo7 and PI31 contain a conserved FP domain that mediates the homo-/hetero-dimerization of the proteins. The PI31 FP domain may also interact with the F-box motif in Fbxo7. The FP domain-mediated protein-protein interactions are important for the functions of Fbxo7 and PI31. The crystal structures of the Fbxo7 and PI31 FP domains were determined previously, showing that a C-terminal helix in the Fbxo7 FP domain was not present in the PI31 FP domain. Here, we determine the crystal structure of the PI31 FP domain using a longer protein construct. The structure is comparable to the Fbxo7 FP domain (including the C-terminal helix), indicating that the two FP domains share the same global fold. However, the FP domains also harbor their own characteristic structural features, mainly in the longest loop (which has a largely fixed conformation due to extensive hydrogen bonding and hydrophobic interactions) and the C-terminal end regions. The crystal structures also reveal fundamental differences in the modes of protein-protein interactions mediated by the two FP domains: the PI31 FP domain utilizes either an alpha interface or beta interface for homodimeric interaction, whereas the Fbxo7 FP domain utilizes an alphabeta interface. We perform modeling studies to show that the domain-specific structural features may dictate specific modes of inter-domain interactions. We propose that a heterodimeric interaction would be mediated by an alphabeta interface consisting of the alpha-helical and beta-sheet surfaces of the Fbxo7 and PI31 FP domains, respectively. We also discuss the structural/functional significance of various modes of FP domain-mediated protein-protein interactions.
-
-	The FP domains of PI31 and Fbxo7 have the same protein fold but very different modes of protein-protein interaction.,Shang J, Huang X, Du Z J Biomol Struct Dyn. 2014 Sep 30:1-11. PMID:25266262<ref>PMID:25266262</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4ouh" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:46, 25 January 2023

OCA — Wed, 25 Jan 2023 07:46:47 GMT

←Older revision		Revision as of 07:46, 25 January 2023
Line 3:		Line 3:
	<StructureSection load='4ouh' size='340' side='right'caption='[[4ouh]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4ouh' size='340' side='right'caption='[[4ouh]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ouh]] is a 4 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=4OUH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4OUH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ouh]] is a 4 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=4OUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OUH FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HUMAN PI31, PSMF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</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=4ouh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ouh OCA], [https://pdbe.org/4ouh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ouh RCSB], [https://www.ebi.ac.uk/pdbsum/4ouh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ouh ProSAT]</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=4ouh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ouh OCA], [~~http~~://pdbe.org/4ouh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ouh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ouh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ouh ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PSMF1_HUMAN PSMF1_HUMAN]] Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.<ref>PMID:10764772</ref>	+	[https://www.uniprot.org/uniprot/PSMF1_HUMAN PSMF1_HUMAN] Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.<ref>PMID:10764772</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Du, Z]]	+	[[Category: Du Z]]
-	[[Category: Huang, X]]	+	[[Category: Huang X]]
-	[[Category: Shang, J]]	+	[[Category: Shang J]]
-	~~[[Category: C-terminal extention alpha helix]]~~	+
-	~~[[Category: Proteasome inhibitor]]~~	+
-	~~[[Category: Protein binding~~]]	+

OCA at 08:09, 17 April 2019

OCA — Wed, 17 Apr 2019 08:09:56 GMT

←Older revision		Revision as of 08:09, 17 April 2019
Line 1:		Line 1:

	==Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor==		==Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor==
-	<StructureSection load='4ouh' size='340' side='right' caption='[[4ouh]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4ouh' size='340' side='right'caption='[[4ouh]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ouh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OUH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ouh]] is a 4 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=4OUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OUH FirstGlance]. <br>
-	</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=4ouh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ouh OCA], [http://pdbe.org/4ouh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ouh RCSB], [http://www.ebi.ac.uk/pdbsum/4ouh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ouh ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HUMAN PI31, PSMF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4ouh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ouh OCA], [http://pdbe.org/4ouh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ouh RCSB], [http://www.ebi.ac.uk/pdbsum/4ouh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ouh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Du, Z]]		[[Category: Du, Z]]
	[[Category: Huang, X]]		[[Category: Huang, X]]

OCA at 17:32, 9 March 2017

OCA — Thu, 09 Mar 2017 17:32:16 GMT

←Older revision		Revision as of 17:32, 9 March 2017
Line 1:		Line 1:
		+
	==Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor==		==Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor==
	<StructureSection load='4ouh' size='340' side='right' caption='[[4ouh]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4ouh' size='340' side='right' caption='[[4ouh]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ouh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OUH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ouh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OUH FirstGlance]. <br>
-	</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=4ouh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ouh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ouh RCSB], [http://www.ebi.ac.uk/pdbsum/4ouh PDBsum]</span></td></tr>	+	</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=4ouh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ouh OCA], [http://pdbe.org/4ouh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ouh RCSB], [http://www.ebi.ac.uk/pdbsum/4ouh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ouh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4ouh" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:55, 25 February 2015

OCA — Wed, 25 Feb 2015 13:55:46 GMT

←Older revision		Revision as of 13:55, 25 February 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor==
		+	<StructureSection load='4ouh' size='340' side='right' caption='[[4ouh]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4ouh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OUH FirstGlance]. <br>
		+	</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=4ouh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ouh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ouh RCSB], [http://www.ebi.ac.uk/pdbsum/4ouh PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PSMF1_HUMAN PSMF1_HUMAN]] Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.<ref>PMID:10764772</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Fbxo7 and PI31 contain a conserved FP domain that mediates the homo-/hetero-dimerization of the proteins. The PI31 FP domain may also interact with the F-box motif in Fbxo7. The FP domain-mediated protein-protein interactions are important for the functions of Fbxo7 and PI31. The crystal structures of the Fbxo7 and PI31 FP domains were determined previously, showing that a C-terminal helix in the Fbxo7 FP domain was not present in the PI31 FP domain. Here, we determine the crystal structure of the PI31 FP domain using a longer protein construct. The structure is comparable to the Fbxo7 FP domain (including the C-terminal helix), indicating that the two FP domains share the same global fold. However, the FP domains also harbor their own characteristic structural features, mainly in the longest loop (which has a largely fixed conformation due to extensive hydrogen bonding and hydrophobic interactions) and the C-terminal end regions. The crystal structures also reveal fundamental differences in the modes of protein-protein interactions mediated by the two FP domains: the PI31 FP domain utilizes either an alpha interface or beta interface for homodimeric interaction, whereas the Fbxo7 FP domain utilizes an alphabeta interface. We perform modeling studies to show that the domain-specific structural features may dictate specific modes of inter-domain interactions. We propose that a heterodimeric interaction would be mediated by an alphabeta interface consisting of the alpha-helical and beta-sheet surfaces of the Fbxo7 and PI31 FP domains, respectively. We also discuss the structural/functional significance of various modes of FP domain-mediated protein-protein interactions.

-	The ~~entry 4ouh is ON HOLD until Paper Publication~~	+	The FP domains of PI31 and Fbxo7 have the same protein fold but very different modes of protein-protein interaction.,Shang J, Huang X, Du Z J Biomol Struct Dyn. 2014 Sep 30:1-11. PMID:25266262<ref>PMID:25266262</ref>

-	~~Authors: Shang~~, J.~~, Huang, X~~.~~, Du, Z~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor~~	+	== References ==
-	~~[[Category: Unreleased Structures]]~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Du, Z]]		[[Category: Du, Z]]
		+	[[Category: Huang, X]]
	[[Category: Shang, J]]		[[Category: Shang, J]]
-	[[Category: ~~Huang, X~~]]	+	[[Category: C-terminal extention alpha helix]]
		+	[[Category: Proteasome inhibitor]]
		+	[[Category: Protein binding]]

OCA at 14:34, 24 December 2014

OCA — Wed, 24 Dec 2014 14:34:55 GMT

←Older revision		Revision as of 14:34, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor		Description: Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor
		+	[[Category: Unreleased Structures]]
		+	[[Category: Du, Z]]
		+	[[Category: Shang, J]]
		+	[[Category: Huang, X]]

OCA at 06:13, 8 October 2014

OCA — Wed, 08 Oct 2014 06:13:35 GMT

←Older revision		Revision as of 06:13, 8 October 2014
Line 3:		Line 3:
	The entry 4ouh is ON HOLD until Paper Publication		The entry 4ouh is ON HOLD until Paper Publication

-	Authors: Shang,J., Huang,X., Du,Z.	+	Authors: Shang, J., Huang, X., Du, Z.

	Description: Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor		Description: Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor

OCA at 05:50, 9 April 2014

OCA — Wed, 09 Apr 2014 05:50:23 GMT

←Older revision		Revision as of 05:50, 9 April 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ouh is ON HOLD	+	The entry 4ouh is ON HOLD until Paper Publication

	Authors: Shang,J., Huang,X., Du,Z.		Authors: Shang,J., Huang,X., Du,Z.

	Description: Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor		Description: Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor

OCA: Protected "4ouh" [edit=sysop:move=sysop]

OCA — Mon, 03 Mar 2014 16:52:42 GMT

Protected "4ouh" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:52, 3 March 2014

OCA: New page: '''Unreleased structure''' The entry 4ouh is ON HOLD Authors: Shang,J., Huang,X., Du,Z. Description: Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor

OCA — Mon, 03 Mar 2014 16:52:41 GMT

New page: '''Unreleased structure''' The entry 4ouh is ON HOLD Authors: Shang,J., Huang,X., Du,Z. Description: Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor

New page

'''Unreleased structure'''

The entry 4ouh is ON HOLD

Authors: Shang,J., Huang,X., Du,Z.

Description: Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor