2l9v - Revision history

OCA at 06:54, 1 May 2024

OCA — Wed, 01 May 2024 06:54:42 GMT

←Older revision		Revision as of 06:54, 1 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L9V FirstGlance]. <br>		<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L9V 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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [https://pdbe.org/2l9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [https://www.ebi.ac.uk/pdbsum/2l9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9v ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [https://pdbe.org/2l9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [https://www.ebi.ac.uk/pdbsum/2l9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9v ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/PR40A_HUMAN PR40A_HUMAN] Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.<ref>PMID:21834987</ref>		[https://www.uniprot.org/uniprot/PR40A_HUMAN PR40A_HUMAN] Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.<ref>PMID:21834987</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Several all-helical single-domain proteins have been shown to fold rapidly (microsecond time scale) to a compact intermediate state and subsequently rearrange more slowly to the native conformation. An understanding of this process has been hindered by difficulties in experimental studies of intermediates in cases where they are both low-populated and only transiently formed. One such example is provided by the on-pathway folding intermediate of the small four-helix bundle FF domain from HYPA/FBP11 that is populated at several percent with a millisecond lifetime at room temperature. Here we have studied the L24A mutant that has been shown previously to form nonnative interactions in the folding transition state. A suite of Carr-Purcell-Meiboom-Gill relaxation dispersion NMR experiments have been used to measure backbone chemical shifts and amide bond vector orientations of the invisible folding intermediate that form the input restraints in calculations of atomic resolution models of its structure. Despite the fact that the intermediate structure has many features that are similar to that of the native state, a set of nonnative contacts is observed that is even more extensive than noted previously for the wild-type (WT) folding intermediate. Such nonnative interactions, which must be broken prior to adoption of the native conformation, explain why the transition from the intermediate state to the native conformer (millisecond time scale) is significantly slower than from the unfolded ensemble to the intermediate and why the L24A mutant folds more slowly than the WT.
-
-	Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study.,Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE J Am Chem Soc. 2011 Jul 20;133(28):10974-82. Epub 2011 Jun 28. PMID:21639149<ref>PMID:21639149</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2l9v" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:27, 18 January 2023

OCA — Wed, 18 Jan 2023 08:27:44 GMT

←Older revision		Revision as of 08:27, 18 January 2023
Line 1:		Line 1:

	==NMR structure of the FF domain L24A mutant's folding transition state==		==NMR structure of the FF domain L24A mutant's folding transition state==
-	<StructureSection load='2l9v' size='340' side='right'caption='[[2l9v~~]], [[NMR_Ensembles_of_Models \| 9 NMR models~~]]' scene=''>	+	<StructureSection load='2l9v' size='340' side='right'caption='[[2l9v]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L9V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L9V FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FBP11, FLAF1, FNBP3, HIP10, HSPC225, HYPA, PRPF40A ([https://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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [https://pdbe.org/2l9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [https://www.ebi.ac.uk/pdbsum/2l9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9v 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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [https://pdbe.org/2l9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [https://www.ebi.ac.uk/pdbsum/2l9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9v ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PR40A_HUMAN PR40A_HUMAN]] Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.<ref>PMID:21834987</ref>	+	[https://www.uniprot.org/uniprot/PR40A_HUMAN PR40A_HUMAN] Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.<ref>PMID:21834987</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: Baker, D]]	+	[[Category: Baker D]]
-	[[Category: Fersht~~, A R~~]]	+	[[Category: Fersht AR]]
-	[[Category: Hansen, A]]	+	[[Category: Hansen A]]
-	[[Category: Kay~~, L E~~]]	+	[[Category: Kay LE]]
-	[[Category: Korzhnev~~, D M~~]]	+	[[Category: Korzhnev DM]]
-	[[Category: Religa~~, T L~~]]	+	[[Category: Religa TL]]
-	[[Category: Vernon~~, R M]]~~	+	[[Category: Vernon RM]]
-	~~[[Category: Rna binding protein~~]]	+

OCA at 07:38, 14 April 2021

OCA — Wed, 14 Apr 2021 07:38:56 GMT

←Older revision		Revision as of 07:38, 14 April 2021
Line 1:		Line 1:

	==NMR structure of the FF domain L24A mutant's folding transition state==		==NMR structure of the FF domain L24A mutant's folding transition state==
-	<StructureSection load='2l9v' size='340' side='right' caption='[[2l9v]], [[NMR_Ensembles_of_Models \| 9 NMR models]]' scene=''>	+	<StructureSection load='2l9v' size='340' side='right'caption='[[2l9v]], [[NMR_Ensembles_of_Models \| 9 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2L9V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L9V FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FBP11, FLAF1, FNBP3, HIP10, HSPC225, HYPA, PRPF40A ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FBP11, FLAF1, FNBP3, HIP10, HSPC225, HYPA, PRPF40A ([https://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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [~~http~~://pdbe.org/2l9v PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2l9v PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9v 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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [https://pdbe.org/2l9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [https://www.ebi.ac.uk/pdbsum/2l9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9v ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PR40A_HUMAN PR40A_HUMAN]] Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.<ref>PMID:21834987</ref>	+	[[https://www.uniprot.org/uniprot/PR40A_HUMAN PR40A_HUMAN]] Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.<ref>PMID:21834987</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Baker, D]]		[[Category: Baker, D]]
	[[Category: Fersht, A R]]		[[Category: Fersht, A R]]

OCA at 19:35, 1 August 2018

OCA — Wed, 01 Aug 2018 19:35:18 GMT

←Older revision		Revision as of 19:35, 1 August 2018
Line 5:		Line 5:
	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L9V FirstGlance]. <br>		<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L9V FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FBP11, FLAF1, FNBP3, HIP10, HSPC225, HYPA, PRPF40A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FBP11, FLAF1, FNBP3, HIP10, HSPC225, HYPA, PRPF40A ([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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://pdbe.org/2l9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://pdbe.org/2l9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9v ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 18:17, 10 May 2016

OCA — Tue, 10 May 2016 18:17:14 GMT

←Older revision		Revision as of 18:17, 10 May 2016
Line 1:		Line 1:
		+
	==NMR structure of the FF domain L24A mutant's folding transition state==		==NMR structure of the FF domain L24A mutant's folding transition state==
	<StructureSection load='2l9v' size='340' side='right' caption='[[2l9v]], [[NMR_Ensembles_of_Models \| 9 NMR models]]' scene=''>		<StructureSection load='2l9v' size='340' side='right' caption='[[2l9v]], [[NMR_Ensembles_of_Models \| 9 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L9V FirstGlance]. <br>		<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L9V FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">~~PRPF40A,~~ FBP11, FLAF1, FNBP3, HIP10, HYPA, ~~HSPC225~~ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FBP11, FLAF1, FNBP3, HIP10, HSPC225, HYPA, PRPF40A ([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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://pdbe.org/2l9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://pdbe.org/2l9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</span></td></tr>
	</table>		</table>

OCA at 18:34, 10 September 2015

OCA — Thu, 10 Sep 2015 18:34:00 GMT

←Older revision		Revision as of 18:34, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2l9v' size='340' side='right' caption='[[2l9v]], [[NMR_Ensembles_of_Models \| 9 NMR models]]' scene=''>		<StructureSection load='2l9v' size='340' side='right' caption='[[2l9v]], [[NMR_Ensembles_of_Models \| 9 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L9V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L9V FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRPF40A, FBP11, FLAF1, FNBP3, HIP10, HYPA, HSPC225 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRPF40A, FBP11, FLAF1, FNBP3, HIP10, HYPA, HSPC225 ([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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://pdbe.org/2l9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		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 2l9v" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Baker, D]]		[[Category: Baker, D]]
	[[Category: Fersht, A R]]		[[Category: Fersht, A R]]

OCA at 04:23, 25 December 2014

OCA — Thu, 25 Dec 2014 04:23:08 GMT

←Older revision		Revision as of 04:23, 25 December 2014
Line 6:		Line 6:
	<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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PR40A_HUMAN PR40A_HUMAN]] Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.<ref>PMID:21834987</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 06:09, 22 December 2014

OCA — Mon, 22 Dec 2014 06:09:31 GMT

←Older revision		Revision as of 06:09, 22 December 2014
Line 2:		Line 2:
	<StructureSection load='2l9v' size='340' side='right' caption='[[2l9v]], [[NMR_Ensembles_of_Models \| 9 NMR models]]' scene=''>		<StructureSection load='2l9v' size='340' side='right' caption='[[2l9v]], [[NMR_Ensembles_of_Models \| 9 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. <br>	+	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L9V FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRPF40A, FBP11, FLAF1, FNBP3, HIP10, HYPA, HSPC225 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRPF40A, FBP11, FLAF1, FNBP3, HIP10, HYPA, HSPC225 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr~~><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class~~='~~plainlinks~~'~~>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</span></td></tr>
-	~~<tr~~><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</span></td></tr>	+	</table>
-	<table>	+
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 13:		Line 12:
	Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study.,Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE J Am Chem Soc. 2011 Jul 20;133(28):10974-82. Epub 2011 Jun 28. PMID:21639149<ref>PMID:21639149</ref>		Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study.,Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE J Am Chem Soc. 2011 Jul 20;133(28):10974-82. Epub 2011 Jun 28. PMID:21639149<ref>PMID:21639149</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 20:		Line 19:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Baker, D.]]	+	[[Category: Baker, D]]
-	[[Category: Fersht, A R.]]	+	[[Category: Fersht, A R]]
-	[[Category: Hansen, A.]]	+	[[Category: Hansen, A]]
-	[[Category: Kay, L E.]]	+	[[Category: Kay, L E]]
-	[[Category: Korzhnev, D M.]]	+	[[Category: Korzhnev, D M]]
-	[[Category: Religa, T L.]]	+	[[Category: Religa, T L]]
-	[[Category: Vernon, R M.]]	+	[[Category: Vernon, R M]]
	[[Category: Rna binding protein]]		[[Category: Rna binding protein]]

OCA at 09:55, 1 May 2014

OCA — Thu, 01 May 2014 09:55:25 GMT

←Older revision		Revision as of 09:55, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='2l9v' size='340' side='right' caption='[[2l9v]], [[NMR_Ensembles_of_Models \| 9 NMR models]]' scene=''>		<StructureSection load='2l9v' size='340' side='right' caption='[[2l9v]], [[NMR_Ensembles_of_Models \| 9 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. <br>	+	<table><tr><td colspan='2'>[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. <br>
-	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>	+	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRPF40A, FBP11, FLAF1, FNBP3, HIP10, HYPA, HSPC225 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</span><br>	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	Several all-helical single-domain proteins have been shown to fold rapidly (microsecond time scale) to a compact intermediate state and subsequently rearrange more slowly to the native conformation. An understanding of this process has been hindered by difficulties in experimental studies of intermediates in cases where they are both low-populated and only transiently formed. One such example is provided by the on-pathway folding intermediate of the small four-helix bundle FF domain from HYPA/FBP11 that is populated at several percent with a millisecond lifetime at room temperature. Here we have studied the L24A mutant that has been shown previously to form nonnative interactions in the folding transition state. A suite of Carr-Purcell-Meiboom-Gill relaxation dispersion NMR experiments have been used to measure backbone chemical shifts and amide bond vector orientations of the invisible folding intermediate that form the input restraints in calculations of atomic resolution models of its structure. Despite the fact that the intermediate structure has many features that are similar to that of the native state, a set of nonnative contacts is observed that is even more extensive than noted previously for the wild-type (WT) folding intermediate. Such nonnative interactions, which must be broken prior to adoption of the native conformation, explain why the transition from the intermediate state to the native conformer (millisecond time scale) is significantly slower than from the unfolded ensemble to the intermediate and why the L24A mutant folds more slowly than the WT.		Several all-helical single-domain proteins have been shown to fold rapidly (microsecond time scale) to a compact intermediate state and subsequently rearrange more slowly to the native conformation. An understanding of this process has been hindered by difficulties in experimental studies of intermediates in cases where they are both low-populated and only transiently formed. One such example is provided by the on-pathway folding intermediate of the small four-helix bundle FF domain from HYPA/FBP11 that is populated at several percent with a millisecond lifetime at room temperature. Here we have studied the L24A mutant that has been shown previously to form nonnative interactions in the folding transition state. A suite of Carr-Purcell-Meiboom-Gill relaxation dispersion NMR experiments have been used to measure backbone chemical shifts and amide bond vector orientations of the invisible folding intermediate that form the input restraints in calculations of atomic resolution models of its structure. Despite the fact that the intermediate structure has many features that are similar to that of the native state, a set of nonnative contacts is observed that is even more extensive than noted previously for the wild-type (WT) folding intermediate. Such nonnative interactions, which must be broken prior to adoption of the native conformation, explain why the transition from the intermediate state to the native conformer (millisecond time scale) is significantly slower than from the unfolded ensemble to the intermediate and why the L24A mutant folds more slowly than the WT.
Line 11:		Line 14:

	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:20, 30 April 2014

OCA — Wed, 30 Apr 2014 10:20:11 GMT

←Older revision		Revision as of 10:20, 30 April 2014
Line 4:		Line 4:
	[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. <br>		[[2l9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9V OCA]. <br>
	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>		<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l9v RCSB], [http://www.ebi.ac.uk/pdbsum/2l9v PDBsum]</span><br>
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	Several all-helical single-domain proteins have been shown to fold rapidly (microsecond time scale) to a compact intermediate state and subsequently rearrange more slowly to the native conformation. An understanding of this process has been hindered by difficulties in experimental studies of intermediates in cases where they are both low-populated and only transiently formed. One such example is provided by the on-pathway folding intermediate of the small four-helix bundle FF domain from HYPA/FBP11 that is populated at several percent with a millisecond lifetime at room temperature. Here we have studied the L24A mutant that has been shown previously to form nonnative interactions in the folding transition state. A suite of Carr-Purcell-Meiboom-Gill relaxation dispersion NMR experiments have been used to measure backbone chemical shifts and amide bond vector orientations of the invisible folding intermediate that form the input restraints in calculations of atomic resolution models of its structure. Despite the fact that the intermediate structure has many features that are similar to that of the native state, a set of nonnative contacts is observed that is even more extensive than noted previously for the wild-type (WT) folding intermediate. Such nonnative interactions, which must be broken prior to adoption of the native conformation, explain why the transition from the intermediate state to the native conformer (millisecond time scale) is significantly slower than from the unfolded ensemble to the intermediate and why the L24A mutant folds more slowly than the WT.		Several all-helical single-domain proteins have been shown to fold rapidly (microsecond time scale) to a compact intermediate state and subsequently rearrange more slowly to the native conformation. An understanding of this process has been hindered by difficulties in experimental studies of intermediates in cases where they are both low-populated and only transiently formed. One such example is provided by the on-pathway folding intermediate of the small four-helix bundle FF domain from HYPA/FBP11 that is populated at several percent with a millisecond lifetime at room temperature. Here we have studied the L24A mutant that has been shown previously to form nonnative interactions in the folding transition state. A suite of Carr-Purcell-Meiboom-Gill relaxation dispersion NMR experiments have been used to measure backbone chemical shifts and amide bond vector orientations of the invisible folding intermediate that form the input restraints in calculations of atomic resolution models of its structure. Despite the fact that the intermediate structure has many features that are similar to that of the native state, a set of nonnative contacts is observed that is even more extensive than noted previously for the wild-type (WT) folding intermediate. Such nonnative interactions, which must be broken prior to adoption of the native conformation, explain why the transition from the intermediate state to the native conformer (millisecond time scale) is significantly slower than from the unfolded ensemble to the intermediate and why the L24A mutant folds more slowly than the WT.