1wlq - Revision history

OCA: Redirecting to 2zxx

OCA — Wed, 18 Feb 2009 06:57:03 GMT

Redirecting to 2zxx

←Older revision		Revision as of 06:57, 18 February 2009
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-	~~{{Seed}}~~	+	#REDIRECT [[2zxx]] This PDB entry is obsolete and replaced by 2zxx
-	[[~~Image:1wlq.png\|left\|200px~~]]	+
-		+
-	~~<!--~~	+
-	~~The line below this paragraph, containing "STRUCTURE_1wlq", creates the "Structure Box" on the page.~~	+
-	~~You may change the~~ PDB ~~parameter (which sets the PDB file loaded into the applet)~~	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page~~ is ~~loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display.~~	+
-	~~-->~~	+
-	~~{{STRUCTURE_1wlq\| PDB=1wlq \| SCENE= }}~~	+
-		+
-	~~===Strucure of Geminin-Cdt1 complex===~~	+
-		+
-		+
-	~~<!--~~	+
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_15286659}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at http://www.pubmed.gov), where 15286659 is the PubMed ID number.~~	+
-	~~-->~~	+
-	~~{{ABSTRACT_PUBMED_15286659}}~~	+
-		+
-	~~==About this Structure==~~	+
-	1WLQ is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLQ OCA].	+
-		+
-	~~==Reference==~~	+
-	~~<ref group="xtra">PMID:15286659</ref><references group="xtra"/>~~	+
-	~~[[Category: Mus musculus]]~~	+
-	~~[[Category: Cho, Y.]]~~	+
-	~~[[Category: Choi, J M.]]~~	+
-	~~[[Category: Enomoto, T.]]~~	+
-	~~[[Category: Hong, B.]]~~	+
-	~~[[Category: Ishimi, Y.]]~~	+
-	~~[[Category: Kim, Y.]]~~	+
-	~~[[Category: Lee, C.]]~~	+
-	~~[[Category: Tada, S.]]~~	+
-	~~[[Category: Watanabe, S.]]~~	+
-	~~[[Category: Coiled-coil]]~~	+
-		+
-	~~''Page seeded~~ by ~~[http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 03:01:22 2009''~~	+

OCA at 01:01, 17 February 2009

OCA — Tue, 17 Feb 2009 01:01:27 GMT

←Older revision		Revision as of 01:01, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	1WLQ is a ~~[[Protein complex]]~~ structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLQ OCA].	+	1WLQ is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLQ OCA].

	==Reference==		==Reference==
-	Structural basis for inhibition of the replication licensing factor Cdt1 by geminin., Lee C, Hong B, Choi JM, Kim Y, Watanabe S, Ishimi Y, Enomoto T, Tada S, Kim Y, Cho Y, Nature. 2004 Aug 19;430(7002):913-7. Epub 2004 Aug 1. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/15286659 15286659]~~	+	<ref group="xtra">PMID:15286659</ref><references group="xtra"/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Protein complex]]
	[[Category: Cho, Y.]]		[[Category: Cho, Y.]]
	[[Category: Choi, J M.]]		[[Category: Choi, J M.]]
Line 37:		Line 36:
	[[Category: Coiled-coil]]		[[Category: Coiled-coil]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jul 28 06~~:43:~~47 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 03:01:22 2009''

OCA at 03:43, 28 July 2008

OCA — Mon, 28 Jul 2008 03:43:50 GMT

←Older revision		Revision as of 03:43, 28 July 2008
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-	[[Image:1wlq.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:1wlq.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_1wlq\| PDB=1wlq \| SCENE= }}		{{STRUCTURE_1wlq\| PDB=1wlq \| SCENE= }}

-	~~'''~~Strucure of Geminin-Cdt1 complex~~'''~~	+	===Strucure of Geminin-Cdt1 complex===


-	~~==Overview==~~	+	<!--
-	~~To maintain chromosome stability in eukaryotic cells, replication origins must be licensed by loading mini~~-~~chromosome maintenance (MCM2~~-~~7) complexes once and only once per cell cycle. This licensing control is achieved through the activities of geminin and cyclin-dependent kinases. Geminin binds tightly to Cdt1~~, ~~an essential component of the replication licensing system~~, ~~and prevents~~ the ~~inappropriate reinitiation of replication on an already fired origin. The inhibitory effect of geminin is thought~~ to ~~prevent~~ the ~~interaction between Cdt1 and the MCM helicase~~. ~~Here we describe the crystal structure of the mouse geminin-Cdt1 complex using tGeminin (residues 79-157, truncated geminin~~) ~~and tCdt1 (residues 172-368~~, ~~truncated Cdt1). The amino-terminal region of a coiled-coil dimer of tGeminin interacts with both N-terminal and carboxy-terminal parts of tCdt1. The primary interface relies on~~ the ~~steric complementarity between the tGeminin dimer and the hydrophobic face of the two short N-terminal helices of tCdt1 and, in particular, Pro 181, Ala 182, Tyr 183, Phe 186 and Leu 189~~. ~~The crystal structure, in conjunction with our biochemical data, indicates that the N~~-~~terminal region of tGeminin might be required to anchor tCdt1, and the C~~-~~terminal region of tGeminin prevents access of the MCM complex to tCdt1 through steric hindrance.~~	+	The line below this paragraph, {{ABSTRACT_PUBMED_15286659}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 15286659 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_15286659}}

	==About this Structure==		==About this Structure==
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	[[Category: Watanabe, S.]]		[[Category: Watanabe, S.]]
	[[Category: Coiled-coil]]		[[Category: Coiled-coil]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 13~~:50:50 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:43:47 2008''

OCA at 10:50, 3 May 2008

OCA — Sat, 03 May 2008 10:50:51 GMT

←Older revision		Revision as of 10:50, 3 May 2008
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	[[Image:1wlq.gif\|left\|200px]]		[[Image:1wlq.gif\|left\|200px]]

-	{{Structure	+	<!--
-	\|PDB~~= 1wlq \|SIZE=350\|CAPTION= <~~scene ~~name='initialview01'>1wlq</scene>~~, ~~resolution 2~~.~~80Å~~	+	The line below this paragraph, containing "STRUCTURE_1wlq", creates the "Structure Box" on the page.
-	~~\|SITE=~~	+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	~~\|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene~~>	+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	\|~~ACTIVITY~~=	+	or leave the SCENE parameter empty for the default display.
-	\|~~GENE~~=	+	-->
-	~~\|DOMAIN=~~	+	{{STRUCTURE_1wlq\| PDB=1wlq \| SCENE= }}
-	~~\|RELATEDENTRY=~~	+
-	\|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wlq OCA], [http://www.ebi.ac.uk/pdbsum/1wlq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wlq RCSB]</span>	+
-	}}	+

	'''Strucure of Geminin-Cdt1 complex'''		'''Strucure of Geminin-Cdt1 complex'''
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	[[Category: Tada, S.]]		[[Category: Tada, S.]]
	[[Category: Watanabe, S.]]		[[Category: Watanabe, S.]]
-	[[Category: ~~coiled~~-coil]]	+	[[Category: Coiled-coil]]
-		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:50:50 2008''
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Mar 31 00~~:37:55 2008''	+

OCA at 21:37, 30 March 2008

OCA — Sun, 30 Mar 2008 21:37:56 GMT

←Older revision		Revision as of 21:37, 30 March 2008
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	\|PDB= 1wlq \|SIZE=350\|CAPTION= <scene name='initialview01'>1wlq</scene>, resolution 2.80Å		\|PDB= 1wlq \|SIZE=350\|CAPTION= <scene name='initialview01'>1wlq</scene>, resolution 2.80Å
	\|SITE=		\|SITE=
-	\|LIGAND=	+	\|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
	\|ACTIVITY=		\|ACTIVITY=
	\|GENE=		\|GENE=
		+	\|DOMAIN=
		+	\|RELATEDENTRY=
		+	\|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wlq OCA], [http://www.ebi.ac.uk/pdbsum/1wlq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wlq RCSB]</span>
	}}		}}

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	[[Category: coiled-coil]]		[[Category: coiled-coil]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu~~ Mar ~~20 14~~:58:33 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:37:55 2008''

OCA at 12:58, 20 March 2008

OCA — Thu, 20 Mar 2008 12:58:34 GMT

←Older revision		Revision as of 12:58, 20 March 2008
Line 1:		Line 1:
-	[[Image:1wlq.gif\|left\|200px]]~~<br /><applet load~~="1wlq~~" size~~="350~~" color~~=~~"white" frame="true" align~~=~~"right" spinBox="true"~~	+	[[Image:1wlq.gif\|left\|200px]]
-	~~caption="~~1wlq, resolution 2.80Å~~" />~~	+
-	'''Strucure of Geminin-Cdt1 complex'''~~<br />~~	+	{{Structure
		+	\|PDB= 1wlq \|SIZE=350\|CAPTION= <scene name='initialview01'>1wlq</scene>, resolution 2.80Å
		+	\|SITE=
		+	\|LIGAND=
		+	\|ACTIVITY=
		+	\|GENE=
		+	}}
		+
		+	'''Strucure of Geminin-Cdt1 complex'''
		+

	==Overview==		==Overview==
Line 7:		Line 16:

	==About this Structure==		==About this Structure==
-	1WLQ is a [~~http://en.wikipedia.org/wiki/Protein_complex~~ Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLQ OCA].	+	1WLQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLQ OCA].

	==Reference==		==Reference==
-	Structural basis for inhibition of the replication licensing factor Cdt1 by geminin., Lee C, Hong B, Choi JM, Kim Y, Watanabe S, Ishimi Y, Enomoto T, Tada S, Kim Y, Cho Y, Nature. 2004 Aug 19;430(7002):913-7. Epub 2004 Aug 1. PMID:[http://~~ispc~~.~~weizmann~~.ac.~~il/~~/~~pmbin~~/~~getpm?pmid=~~15286659 15286659]	+	Structural basis for inhibition of the replication licensing factor Cdt1 by geminin., Lee C, Hong B, Choi JM, Kim Y, Watanabe S, Ishimi Y, Enomoto T, Tada S, Kim Y, Cho Y, Nature. 2004 Aug 19;430(7002):913-7. Epub 2004 Aug 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15286659 15286659]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Protein complex]]		[[Category: Protein complex]]
Line 24:		Line 33:
	[[Category: coiled-coil]]		[[Category: coiled-coil]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu ~~Feb 21 15~~:45:42 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:58:33 2008''

OCA at 13:45, 21 February 2008

OCA — Thu, 21 Feb 2008 13:45:43 GMT

←Older revision		Revision as of 13:45, 21 February 2008
Line 1:		Line 1:
-	[[Image:1wlq.gif\|left\|200px]]<br /><applet load="1wlq" size="~~450~~" color="white" frame="true" align="right" spinBox="true"	+	[[Image:1wlq.gif\|left\|200px]]<br /><applet load="1wlq" size="350" color="white" frame="true" align="right" spinBox="true"
	caption="1wlq, resolution 2.80Å" />		caption="1wlq, resolution 2.80Å" />
	'''Strucure of Geminin-Cdt1 complex'''<br />		'''Strucure of Geminin-Cdt1 complex'''<br />

	==Overview==		==Overview==
-	To maintain chromosome stability in eukaryotic cells, replication origins, must be licensed by loading mini-chromosome maintenance (MCM2-7) complexes, once and only once per cell cycle. This licensing control is achieved, through the activities of geminin and cyclin-dependent kinases. Geminin, binds tightly to Cdt1, an essential component of the replication licensing, system, and prevents the inappropriate reinitiation of replication on an, already fired origin. The inhibitory effect of geminin is thought to, prevent the interaction between Cdt1 and the MCM helicase. Here we, describe the crystal structure of the mouse geminin-Cdt1 complex using, tGeminin (residues 79-157, truncated geminin) and tCdt1 (residues 172-368, truncated Cdt1). The amino-terminal region of a coiled-coil dimer of, tGeminin interacts with both N-terminal and carboxy-terminal parts of, tCdt1. The primary interface relies on the steric complementarity between, the tGeminin dimer and the hydrophobic face of the two short N-terminal, helices of tCdt1 and, in particular, Pro 181, Ala 182, Tyr 183, Phe 186, and Leu 189. The crystal structure, in conjunction with our biochemical, data, indicates that the N-terminal region of tGeminin might be required, to anchor tCdt1, and the C-terminal region of tGeminin prevents access of, the MCM complex to tCdt1 through steric hindrance.	+	To maintain chromosome stability in eukaryotic cells, replication origins must be licensed by loading mini-chromosome maintenance (MCM2-7) complexes once and only once per cell cycle. This licensing control is achieved through the activities of geminin and cyclin-dependent kinases. Geminin binds tightly to Cdt1, an essential component of the replication licensing system, and prevents the inappropriate reinitiation of replication on an already fired origin. The inhibitory effect of geminin is thought to prevent the interaction between Cdt1 and the MCM helicase. Here we describe the crystal structure of the mouse geminin-Cdt1 complex using tGeminin (residues 79-157, truncated geminin) and tCdt1 (residues 172-368, truncated Cdt1). The amino-terminal region of a coiled-coil dimer of tGeminin interacts with both N-terminal and carboxy-terminal parts of tCdt1. The primary interface relies on the steric complementarity between the tGeminin dimer and the hydrophobic face of the two short N-terminal helices of tCdt1 and, in particular, Pro 181, Ala 182, Tyr 183, Phe 186 and Leu 189. The crystal structure, in conjunction with our biochemical data, indicates that the N-terminal region of tGeminin might be required to anchor tCdt1, and the C-terminal region of tGeminin prevents access of the MCM complex to tCdt1 through steric hindrance.

	==About this Structure==		==About this Structure==
-	1WLQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1WLQ OCA].	+	1WLQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLQ OCA].

	==Reference==		==Reference==
Line 14:		Line 14:
	[[Category: Protein complex]]		[[Category: Protein complex]]
	[[Category: Cho, Y.]]		[[Category: Cho, Y.]]
-	[[Category: Choi, J.M.]]	+	[[Category: Choi, J M.]]
	[[Category: Enomoto, T.]]		[[Category: Enomoto, T.]]
	[[Category: Hong, B.]]		[[Category: Hong, B.]]
Line 24:		Line 24:
	[[Category: coiled-coil]]		[[Category: coiled-coil]]

-	''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 05:30:~~59 2007~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:42 2008''

OCA: New page: 200px
'''Strucure of Geminin-...
OCA — Wed, 21 Nov 2007 03:23:44 GMT

New page: 200px<br /><applet load="1wlq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wlq, resolution 2.80Å" /> '''Strucure of Geminin-...

New page
[[Image:1wlq.gif|left|200px]]<br /><applet load="1wlq" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1wlq, resolution 2.80Å" />
'''Strucure of Geminin-Cdt1 complex'''<br />

==Overview==
To maintain chromosome stability in eukaryotic cells, replication origins, must be licensed by loading mini-chromosome maintenance (MCM2-7) complexes, once and only once per cell cycle. This licensing control is achieved, through the activities of geminin and cyclin-dependent kinases. Geminin, binds tightly to Cdt1, an essential component of the replication licensing, system, and prevents the inappropriate reinitiation of replication on an, already fired origin. The inhibitory effect of geminin is thought to, prevent the interaction between Cdt1 and the MCM helicase. Here we, describe the crystal structure of the mouse geminin-Cdt1 complex using, tGeminin (residues 79-157, truncated geminin) and tCdt1 (residues 172-368, truncated Cdt1). The amino-terminal region of a coiled-coil dimer of, tGeminin interacts with both N-terminal and carboxy-terminal parts of, tCdt1. The primary interface relies on the steric complementarity between, the tGeminin dimer and the hydrophobic face of the two short N-terminal, helices of tCdt1 and, in particular, Pro 181, Ala 182, Tyr 183, Phe 186, and Leu 189. The crystal structure, in conjunction with our biochemical, data, indicates that the N-terminal region of tGeminin might be required, to anchor tCdt1, and the C-terminal region of tGeminin prevents access of, the MCM complex to tCdt1 through steric hindrance.

==About this Structure==
1WLQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WLQ OCA].

==Reference==
Structural basis for inhibition of the replication licensing factor Cdt1 by geminin., Lee C, Hong B, Choi JM, Kim Y, Watanabe S, Ishimi Y, Enomoto T, Tada S, Kim Y, Cho Y, Nature. 2004 Aug 19;430(7002):913-7. Epub 2004 Aug 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15286659 15286659]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Cho, Y.]]
[[Category: Choi, J.M.]]
[[Category: Enomoto, T.]]
[[Category: Hong, B.]]
[[Category: Ishimi, Y.]]
[[Category: Kim, Y.]]
[[Category: Lee, C.]]
[[Category: Tada, S.]]
[[Category: Watanabe, S.]]
[[Category: coiled-coil]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:30:59 2007''