4lik - Revision history

OCA at 12:19, 1 March 2024

OCA — Fri, 01 Mar 2024 12:19:55 GMT

←Older revision		Revision as of 12:19, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4lik]] 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=4LIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LIK FirstGlance]. <br>		<table><tr><td colspan='2'>[[4lik]] 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=4LIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LIK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.7Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4lik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lik OCA], [https://pdbe.org/4lik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lik RCSB], [https://www.ebi.ac.uk/pdbsum/4lik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lik 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=4lik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lik OCA], [https://pdbe.org/4lik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lik RCSB], [https://www.ebi.ac.uk/pdbsum/4lik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lik ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/PRI1_HUMAN PRI1_HUMAN] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.		[https://www.uniprot.org/uniprot/PRI1_HUMAN PRI1_HUMAN] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	DNA replication in all organisms requires polymerases to synthesize copies of the genome. DNA polymerases are unable to function on a bare template and require a primer. Primases are crucial RNA polymerases that perform the initial de novo synthesis, generating the first 8-10 nucleotides of the primer. Although structures of archaeal and bacterial primases have provided insights into general priming mechanisms, these proteins are not well conserved with heterodimeric (p48/p58) primases in eukaryotes. Here, we present X-ray crystal structures of the catalytic engine of a eukaryotic primase, which is contained in the p48 subunit. The structures of p48 reveal that eukaryotic primases maintain the conserved catalytic prim fold domain, but with a unique subdomain not found in the archaeal and bacterial primases. Calorimetry experiments reveal that Mn2+ but not Mg2+ significantly enhances the binding of nucleotide to primase, which correlates with higher catalytic efficiency in vitro. The structure of p48 with bound UTP and Mn2+ provides insights into the mechanism of nucleotide synthesis by primase. Substitution of conserved residues involved in either metal or nucleotide binding alter nucleotide binding affinities, and yeast strains containing the corresponding Pri1p substitutions are not viable. Our results reveal that two residues (S160 and H166) in direct contact with the nucleotide were previously unrecognized as critical to the human primase active site. Comparing p48 structures to those of similar polymerases in different states of action suggests changes that would be required to attain a catalytically competent conformation capable of initiating dinucleotide synthesis.
-
-	Insights into Eukaryotic Primer Synthesis from Structures of the p48 Subunit of Human DNA Primase.,Vaithiyalingam S, Arnett DR, Aggarwal A, Eichman BF, Fanning E, Chazin WJ J Mol Biol. 2013 Nov 13. pii: S0022-2836(13)00718-3. doi:, 10.1016/j.jmb.2013.11.007. PMID:24239947<ref>PMID:24239947</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4lik" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[RNA polymerase 3D structures\|RNA polymerase 3D structures]]		*[[RNA polymerase 3D structures\|RNA polymerase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:03, 14 December 2022

OCA — Wed, 14 Dec 2022 11:03:30 GMT

←Older revision		Revision as of 11:03, 14 December 2022
Line 1:		Line 1:

	==Crystal structure of the catalytic subunit of human primase==		==Crystal structure of the catalytic subunit of human primase==
-	<StructureSection load='4lik' size='340' side='right' caption='[[4lik]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='4lik' size='340' side='right'caption='[[4lik]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4lik]] 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=4LIK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4LIK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4lik]] 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=4LIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LIK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lil\|4lil]], [[4lim\|4lim]]</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=4lik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lik OCA], [https://pdbe.org/4lik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lik RCSB], [https://www.ebi.ac.uk/pdbsum/4lik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lik ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRIM1 ([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=4lik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lik OCA], [~~http~~://pdbe.org/4lik PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4lik RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4lik PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4lik ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PRI1_HUMAN PRI1_HUMAN]] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.	+	[https://www.uniprot.org/uniprot/PRI1_HUMAN PRI1_HUMAN] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
-	*[[RNA polymerase\|RNA polymerase]]	+	*[[RNA polymerase 3D structures\|RNA polymerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Chazin, W J~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Eichman, B F~~]]	+	[[Category: Chazin WJ]]
-	[[Category: ~~Vaithiyalingam, S~~]]	+	[[Category: Eichman BF]]
-	[[Category: ~~Prim fold]]~~	+	[[Category: Vaithiyalingam S]]
-	~~[[Category: Transferase~~]]	+

OCA at 14:29, 4 August 2016

OCA — Thu, 04 Aug 2016 14:29:23 GMT

←Older revision		Revision as of 14:29, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the catalytic subunit of human primase==		==Crystal structure of the catalytic subunit of human primase==
	<StructureSection load='4lik' size='340' side='right' caption='[[4lik]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4lik' size='340' side='right' caption='[[4lik]], [[Resolution\|resolution]] 1.70Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lil\|4lil]], [[4lim\|4lim]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lil\|4lil]], [[4lim\|4lim]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRIM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRIM1 ([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=4lik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lik OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lik RCSB], [http://www.ebi.ac.uk/pdbsum/4lik 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=4lik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lik OCA], [http://pdbe.org/4lik PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lik RCSB], [http://www.ebi.ac.uk/pdbsum/4lik PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lik ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4lik" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 15:47, 24 December 2014

OCA — Wed, 24 Dec 2014 15:47:43 GMT

←Older revision		Revision as of 15:47, 24 December 2014
Line 8:		Line 8:
	<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=4lik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lik OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lik RCSB], [http://www.ebi.ac.uk/pdbsum/4lik 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=4lik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lik OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lik RCSB], [http://www.ebi.ac.uk/pdbsum/4lik PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PRI1_HUMAN PRI1_HUMAN]] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 18:59, 21 December 2014

OCA — Sun, 21 Dec 2014 18:59:11 GMT

←Older revision		Revision as of 18:59, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4lik\| PDB~~=4lik \| ~~SCENE~~= }}	+	==Crystal structure of the catalytic subunit of human primase==
-	===~~Crystal~~ structure of the catalytic subunit of human primase~~===~~	+	<StructureSection load='4lik' size='340' side='right' caption='[[4lik]], [[Resolution\|resolution]] 1.70Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24239947}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4lik]] 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=4LIK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LIK FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lil\|4lil]], [[4lim\|4lim]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PRIM1 ([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=4lik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lik OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lik RCSB], [http://www.ebi.ac.uk/pdbsum/4lik PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	DNA replication in all organisms requires polymerases to synthesize copies of the genome. DNA polymerases are unable to function on a bare template and require a primer. Primases are crucial RNA polymerases that perform the initial de novo synthesis, generating the first 8-10 nucleotides of the primer. Although structures of archaeal and bacterial primases have provided insights into general priming mechanisms, these proteins are not well conserved with heterodimeric (p48/p58) primases in eukaryotes. Here, we present X-ray crystal structures of the catalytic engine of a eukaryotic primase, which is contained in the p48 subunit. The structures of p48 reveal that eukaryotic primases maintain the conserved catalytic prim fold domain, but with a unique subdomain not found in the archaeal and bacterial primases. Calorimetry experiments reveal that Mn2+ but not Mg2+ significantly enhances the binding of nucleotide to primase, which correlates with higher catalytic efficiency in vitro. The structure of p48 with bound UTP and Mn2+ provides insights into the mechanism of nucleotide synthesis by primase. Substitution of conserved residues involved in either metal or nucleotide binding alter nucleotide binding affinities, and yeast strains containing the corresponding Pri1p substitutions are not viable. Our results reveal that two residues (S160 and H166) in direct contact with the nucleotide were previously unrecognized as critical to the human primase active site. Comparing p48 structures to those of similar polymerases in different states of action suggests changes that would be required to attain a catalytically competent conformation capable of initiating dinucleotide synthesis.

-	~~==Function==~~	+	Insights into Eukaryotic Primer Synthesis from Structures of the p48 Subunit of Human DNA Primase.,Vaithiyalingam S, Arnett DR, Aggarwal A, Eichman BF, Fanning E, Chazin WJ J Mol Biol. 2013 Nov 13. pii: S0022-2836(13)00718-3. doi:, 10.1016/j.jmb.2013.11.007. PMID:24239947<ref>PMID:24239947</ref>
-	~~[[http~~:~~//www~~.~~uniprot~~.~~org~~/~~uniprot/PRI1_HUMAN PRI1_HUMAN]] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4lik]] is~~ a ~~1 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4LIK OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:024239947</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[RNA polymerase\|RNA polymerase]]
-	[[Category: Chazin, W J.]]	+	== References ==
-	[[Category: Eichman, B F.]]	+	<references/>
-	[[Category: Vaithiyalingam, S.]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Chazin, W J]]
		+	[[Category: Eichman, B F]]
		+	[[Category: Vaithiyalingam, S]]
	[[Category: Prim fold]]		[[Category: Prim fold]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 13:41, 11 December 2013

OCA — Wed, 11 Dec 2013 13:41:16 GMT

←Older revision		Revision as of 13:41, 11 December 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4lik\| PDB=4lik \| SCENE= }}
		+	===Crystal structure of the catalytic subunit of human primase===
		+	{{ABSTRACT_PUBMED_24239947}}

-	~~The entry 4lik~~ is ~~ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/PRI1_HUMAN PRI1_HUMAN]] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.

-	~~Authors: Vaithiyalingam, S~~.~~, Eichman, B~~.F.~~, Chazin, W~~.J.	+	==About this Structure==
		+	[[4lik]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LIK OCA].

-	~~Description~~: ~~Crystal structure of the catalytic subunit of human primase~~	+	==Reference==
		+	<ref group="xtra">PMID:024239947</ref><references group="xtra"/><references/>
		+	[[Category: Chazin, W J.]]
		+	[[Category: Eichman, B F.]]
		+	[[Category: Vaithiyalingam, S.]]
		+	[[Category: Prim fold]]
		+	[[Category: Transferase]]

OCA at 03:30, 20 September 2013

OCA — Fri, 20 Sep 2013 03:30:24 GMT

←Older revision		Revision as of 03:30, 20 September 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Vaithiyalingam, S., Eichman, B.F., Chazin, W.J.		Authors: Vaithiyalingam, S., Eichman, B.F., Chazin, W.J.

	Description: Crystal structure of the catalytic subunit of human primase		Description: Crystal structure of the catalytic subunit of human primase

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

OCA — Wed, 10 Jul 2013 15:12:01 GMT

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

←Older revision

Revision as of 15:12, 10 July 2013

OCA: New page: '''Unreleased structure''' The entry 4lik is ON HOLD Authors: Vaithiyalingam, S., Eichman, B.F., Chazin, W.J. Description: Crystal structure of the catalytic subunit of human primase

OCA — Wed, 10 Jul 2013 15:12:00 GMT

New page: '''Unreleased structure''' The entry 4lik is ON HOLD Authors: Vaithiyalingam, S., Eichman, B.F., Chazin, W.J. Description: Crystal structure of the catalytic subunit of human primase

New page

'''Unreleased structure'''

The entry 4lik is ON HOLD

Authors: Vaithiyalingam, S., Eichman, B.F., Chazin, W.J.

Description: Crystal structure of the catalytic subunit of human primase