4ipg - Revision history

OCA at 15:28, 20 September 2023

OCA — Wed, 20 Sep 2023 15:28:28 GMT

←Older revision		Revision as of 15:28, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ipg]] is a 1 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=4IPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IPG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ipg]] is a 1 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=4IPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IPG 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=4ipg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ipg OCA], [https://pdbe.org/4ipg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ipg RCSB], [https://www.ebi.ac.uk/pdbsum/4ipg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ipg 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]] 1.58Å</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=4ipg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ipg OCA], [https://pdbe.org/4ipg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ipg RCSB], [https://www.ebi.ac.uk/pdbsum/4ipg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ipg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 21:02, 16 November 2022

OCA — Wed, 16 Nov 2022 21:02:16 GMT

←Older revision		Revision as of 21:02, 16 November 2022
Line 1:		Line 1:

	==Structure of the N-terminal domain of RPA70, E7R, E100R mutant==		==Structure of the N-terminal domain of RPA70, E7R, E100R mutant==
-	<StructureSection load='4ipg' size='340' side='right' caption='[[4ipg]], [[Resolution\|resolution]] 1.58Å' scene=''>	+	<StructureSection load='4ipg' size='340' side='right'caption='[[4ipg]], [[Resolution\|resolution]] 1.58Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ipg]] is a 1 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=4IPG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4IPG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ipg]] is a 1 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=4IPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IPG FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ipc\|4ipc]], [[4ipd\|4ipd]], [[4iph\|4iph]]</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=4ipg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ipg OCA], [https://pdbe.org/4ipg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ipg RCSB], [https://www.ebi.ac.uk/pdbsum/4ipg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ipg ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RPA1, REPA1, RPA70 ([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=4ipg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ipg OCA], [~~http~~://pdbe.org/4ipg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ipg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ipg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ipg ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN]] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref>	+	[https://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 19:

	==See Also==		==See Also==
-	*[[Single-stranded DNA-binding protein\|Single-stranded DNA-binding protein]]	+	*[[Single-stranded DNA-binding protein 3D structures\|Single-stranded DNA-binding protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Chazin, W J~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Feldkamp, M D~~]]	+	[[Category: Chazin WJ]]
-	[[Category: ~~Fesik, S W~~]]	+	[[Category: Feldkamp MD]]
-	[[Category: ~~Frank, A O~~]]	+	[[Category: Fesik SW]]
-	[[Category: ~~Vangamudi, B~~]]	+	[[Category: Frank AO]]
-	[[Category: ~~Ob-fold]]~~	+	[[Category: Vangamudi B]]
-	~~[[Category: Protein binding~~]]	+

OCA at 08:21, 4 August 2016

OCA — Thu, 04 Aug 2016 08:21:19 GMT

←Older revision		Revision as of 08:21, 4 August 2016
Line 1:		Line 1:
		+
	==Structure of the N-terminal domain of RPA70, E7R, E100R mutant==		==Structure of the N-terminal domain of RPA70, E7R, E100R mutant==
	<StructureSection load='4ipg' size='340' side='right' caption='[[4ipg]], [[Resolution\|resolution]] 1.58Å' scene=''>		<StructureSection load='4ipg' size='340' side='right' caption='[[4ipg]], [[Resolution\|resolution]] 1.58Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ipg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IPG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IPG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ipg]] is a 1 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=4IPG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IPG FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ipc\|4ipc]], [[4ipd\|4ipd]], [[4iph\|4iph]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ipc\|4ipc]], [[4ipd\|4ipd]], [[4iph\|4iph]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RPA1, REPA1, RPA70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RPA1, REPA1, RPA70 ([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=4ipg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ipg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ipg RCSB], [http://www.ebi.ac.uk/pdbsum/4ipg 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=4ipg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ipg OCA], [http://pdbe.org/4ipg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ipg RCSB], [http://www.ebi.ac.uk/pdbsum/4ipg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ipg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4ipg" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Chazin, W J]]		[[Category: Chazin, W J]]
	[[Category: Feldkamp, M D]]		[[Category: Feldkamp, M D]]

OCA at 07:35, 24 December 2014

OCA — Wed, 24 Dec 2014 07:35:39 GMT

←Older revision		Revision as of 07:35, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4ipg\| PDB=4ipg \| SCENE= }}~~	+	==Structure of the N-terminal domain of RPA70, E7R, E100R mutant==
-	===Structure of the N-terminal domain of RPA70, E7R, E100R mutant===	+	<StructureSection load='4ipg' size='340' side='right' caption='[[4ipg]], [[Resolution\|resolution]] 1.58Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23962067}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4ipg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IPG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IPG FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ipc\|4ipc]], [[4ipd\|4ipd]], [[4iph\|4iph]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RPA1, REPA1, RPA70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4ipg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ipg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ipg RCSB], [http://www.ebi.ac.uk/pdbsum/4ipg PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN]] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref>		[[http://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN]] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Replication protein A (RPA) is the primary single-stranded DNA (ssDNA) binding protein in eukaryotes. The N-terminal domain of the RPA70 subunit (RPA70N) interacts via a basic cleft with a wide range of DNA processing proteins, including several that regulate DNA damage response and repair. Small molecule inhibitors that disrupt these protein-protein interactions are therefore of interest as chemical probes of these critical DNA processing pathways and as inhibitors to counter the upregulation of DNA damage response and repair associated with treatment of cancer patients with radiation or DNA-damaging agents. Determination of three-dimensional structures of protein-ligand complexes is an important step for elaboration of small molecule inhibitors. However, although crystal structures of free RPA70N and an RPA70N-peptide fusion construct have been reported, RPA70N-inhibitor complexes have been recalcitrant to crystallization. Analysis of the P61 lattice of RPA70N crystals led us to hypothesize that the ligand-binding surface was occluded. Surface reengineering to alter key crystal lattice contacts led to the design of RPA70N E7R, E100R, and E7R/E100R mutants. These mutants crystallized in a P212121 lattice that clearly had significant solvent channels open to the critical basic cleft. Analysis of X-ray crystal structures, target peptide binding affinities, and 15N-1H heteronuclear single-quantum coherence nuclear magnetic resonance spectra showed that the mutations do not result in perturbations of the RPA70N ligand-binding surface. The success of the design was demonstrated by determining the structure of RPA70N E7R soaked with a ligand discovered in a previously reported molecular fragment screen. A fluorescence anisotropy competition binding assay revealed this compound can inhibit the interaction of RPA70N with the peptide binding motif from the DNA damage response protein ATRIP. The implications of the results are discussed in the context of ongoing efforts to design RPA70N inhibitors.
		+
		+	Surface Reengineering of RPA70N Enables Cocrystallization with an Inhibitor of the Replication Protein A Interaction Motif of ATR Interacting Protein.,Feldkamp MD, Frank AO, Kennedy JP, Patrone JD, Vangamudi B, Waterson AG, Fesik SW, Chazin WJ Biochemistry. 2013 Sep 6. PMID:23962067<ref>PMID:23962067</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4ipg]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4IPG OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023962067</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Single-stranded DNA-binding protein\|Single-stranded DNA-binding protein]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Chazin, W J.]]	+	[[Category: Chazin, W J]]
-	[[Category: Feldkamp, M D.]]	+	[[Category: Feldkamp, M D]]
-	[[Category: Fesik, S W.]]	+	[[Category: Fesik, S W]]
-	[[Category: Frank, A O.]]	+	[[Category: Frank, A O]]
-	[[Category: Vangamudi, B.]]	+	[[Category: Vangamudi, B]]
	[[Category: Ob-fold]]		[[Category: Ob-fold]]
	[[Category: Protein binding]]		[[Category: Protein binding]]

OCA at 05:24, 12 September 2013

OCA — Thu, 12 Sep 2013 05:24:04 GMT

←Older revision		Revision as of 05:24, 12 September 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4ipg\| PDB=4ipg \| SCENE= }}
		+	===Structure of the N-terminal domain of RPA70, E7R, E100R mutant===
		+	{{ABSTRACT_PUBMED_23962067}}

-	~~The entry 4ipg is ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN]] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref>

-	~~Authors~~: ~~Feldkamp, M~~.D.~~, Frank, A~~.~~O., Vangamudi, B., Fesik, S~~.W.~~, Chazin, W~~.J.	+	==About this Structure==
		+	[[4ipg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IPG OCA].

-	~~Description~~:	+	==Reference==
		+	<ref group="xtra">PMID:023962067</ref><references group="xtra"/><references/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Chazin, W J.]]
		+	[[Category: Feldkamp, M D.]]
		+	[[Category: Fesik, S W.]]
		+	[[Category: Frank, A O.]]
		+	[[Category: Vangamudi, B.]]
		+	[[Category: Ob-fold]]
		+	[[Category: Protein binding]]

OCA at 12:02, 30 January 2013

OCA — Wed, 30 Jan 2013 12:02:48 GMT

←Older revision		Revision as of 12:02, 30 January 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Feldkamp, M.D., Frank, A.O., Vangamudi, B., Fesik, S.W., Chazin, W.J.		Authors: Feldkamp, M.D., Frank, A.O., Vangamudi, B., Fesik, S.W., Chazin, W.J.

	Description:		Description:

OCA at 11:12, 23 January 2013

OCA — Wed, 23 Jan 2013 11:12:44 GMT

←Older revision		Revision as of 11:12, 23 January 2013
Line 5:		Line 5:
	Authors: Feldkamp, M.D., Frank, A.O., Vangamudi, B., Fesik, S.W., Chazin, W.J.		Authors: Feldkamp, M.D., Frank, A.O., Vangamudi, B., Fesik, S.W., Chazin, W.J.

-	Description: ~~Surface engineering of the N-terminal domain of RPA70N to obtain X-ray structures of co-complexes~~	+	Description:

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

OCA — Wed, 16 Jan 2013 08:28:56 GMT

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

←Older revision

Revision as of 08:28, 16 January 2013

OCA: New page: '''Unreleased structure''' The entry 4ipg is ON HOLD Authors: Feldkamp, M.D., Frank, A.O., Vangamudi, B., Fesik, S.W., Chazin, W.J. Description: Surface engineering of the N-terminal d...

OCA — Wed, 16 Jan 2013 08:28:55 GMT

New page: '''Unreleased structure''' The entry 4ipg is ON HOLD Authors: Feldkamp, M.D., Frank, A.O., Vangamudi, B., Fesik, S.W., Chazin, W.J. Description: Surface engineering of the N-terminal d...

New page

'''Unreleased structure'''

The entry 4ipg is ON HOLD

Authors: Feldkamp, M.D., Frank, A.O., Vangamudi, B., Fesik, S.W., Chazin, W.J.

Description: Surface engineering of the N-terminal domain of RPA70N to obtain X-ray structures of co-complexes