2k2i - Revision history

OCA at 06:43, 1 May 2024

OCA — Wed, 01 May 2024 06:43:46 GMT

←Older revision		Revision as of 06:43, 1 May 2024
Line 1:		Line 1:

	==NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)==		==NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)==
-	<StructureSection load='2k2i' size='340' side='right'caption='[[2k2i~~]], [[NMR_Ensembles_of_Models \| 15 NMR models~~]]' scene=''>	+	<StructureSection load='2k2i' size='340' side='right'caption='[[2k2i]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2k2i]] is a 2 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=2K2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K2I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2k2i]] is a 2 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=2K2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K2I FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>CETN2, CALT, CEN2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])~~</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=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [https://pdbe.org/2k2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [https://www.ebi.ac.uk/pdbsum/2k2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2i 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=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [https://pdbe.org/2k2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [https://www.ebi.ac.uk/pdbsum/2k2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CETN2_HUMAN CETN2_HUMAN]] Plays a fundamental role in microtubule-organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CEP110.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> ~~[[https://www.uniprot.org/uniprot/SFI1_HUMAN SFI1_HUMAN]] Plays a role in the dynamic structure of centrosome-associated contractile fibers via its interaction with CETN2.<ref>PMID:16956364</ref>~~	+	[https://www.uniprot.org/uniprot/CETN2_HUMAN CETN2_HUMAN] Plays a fundamental role in microtubule-organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CEP110.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 19:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k2i ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k2i ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Centrin, an EF-hand calcium-binding protein, has been shown to be involved in the duplication of centrosomes, and Sfi1 (Suppressor of fermentation-induced loss of stress resistance protein 1) is one of its centrosomal targets. There are three isoforms of human centrin, but here we only considered centrin 2 (HsCen2). This protein has the ability to bind to any of the approximately 25 repeats of human Sfi1 (hSfi1) with more or less affinity. In this study, we mainly focused on the 17th repeat (R17-hSfi1-20), which presents the highest level of similarity with a well-studied 17-residue peptide (P17-XPC) from human xeroderma pigmentosum complementation group C protein, another centrin target for DNA repair. The only known structure of HsCen2 was resolved in complex with P17-XPC. The 20-residue peptide R17-hSfi1-20 exhibits the motif L8L4W1, which is the reverse of the XPC motif, W1L4L8. Consequently, the dipole of the helix formed by this motif has a reverse orientation. We wished to ascertain the impact of this reversal on the structure, dynamics and affinity of centrin. To address this question, we determined the structure of C-HsCen2 [the C-terminal domain of HsCen2 (T94-Y172)] in complex with R17-hSfi1-20 and monitored its dynamics by NMR, after having verified that the N-terminal domain of HsCen2 does not interact with the peptide. The structure shows that the binding mode is similar to that of P17-XPC. However, we observed a 2 -A translation of the R17-hSfi1-20 helix along its axis, inducing less anchorage in the protein and the disruption of a hydrogen bond between a tryptophan residue in the peptide and a well-conserved nearby glutamate in C-HsCen2. NMR dynamic studies of the complex strongly suggested the existence of an unusual calcium secondary binding mode in calcium-binding loop III, made possible by the uncommon residue composition of this loop. The secondary metal site is only populated at high calcium concentration and depends on the type of bound ligand.
-
-	Structure, dynamics and thermodynamics of the human centrin 2/hSfi1 complex.,Martinez-Sanz J, Kateb F, Assairi L, Blouquit Y, Bodenhausen G, Abergel D, Mouawad L, Craescu CT J Mol Biol. 2010 Jan 8;395(1):191-204. Epub 2009 Oct 24. PMID:19857500<ref>PMID:19857500</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2k2i" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Assairi, L]]	+	[[Category: Assairi L]]
-	[[Category: Blouquit, Y]]	+	[[Category: Blouquit Y]]
-	[[Category: Craescu, C]]	+	[[Category: Craescu C]]
-	[[Category: Duchambon, P]]	+	[[Category: Duchambon P]]
-	[[Category: Martinez-Sanz, J]]	+	[[Category: Martinez-Sanz J]]
-	[[Category: Mouawad, L]]	+	[[Category: Mouawad L]]
-	~~[[Category: Cell cycle]]~~	+
-	~~[[Category: Cell division]]~~	+
-	~~[[Category: Centrin 2]]~~	+
-	~~[[Category: Mitosis]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Sfi1~~]]	+

OCA at 08:06, 7 April 2021

OCA — Wed, 07 Apr 2021 08:06:48 GMT

←Older revision		Revision as of 08:06, 7 April 2021
Line 1:		Line 1:

	==NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)==		==NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)==
-	<StructureSection load='2k2i' size='340' side='right' caption='[[2k2i]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>	+	<StructureSection load='2k2i' size='340' side='right'caption='[[2k2i]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2k2i]] is a 2 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=2K2I OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2K2I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2k2i]] is a 2 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=2K2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K2I FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CETN2, CALT, CEN2 ([~~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">CETN2, CALT, CEN2 ([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=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [~~http~~://pdbe.org/2k2i PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2k2i PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2i 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=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [https://pdbe.org/2k2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [https://www.ebi.ac.uk/pdbsum/2k2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CETN2_HUMAN CETN2_HUMAN]] Plays a fundamental role in microtubule-organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CEP110.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> [[~~http~~://www.uniprot.org/uniprot/SFI1_HUMAN SFI1_HUMAN]] Plays a role in the dynamic structure of centrosome-associated contractile fibers via its interaction with CETN2.<ref>PMID:16956364</ref>	+	[[https://www.uniprot.org/uniprot/CETN2_HUMAN CETN2_HUMAN]] Plays a fundamental role in microtubule-organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CEP110.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> [[https://www.uniprot.org/uniprot/SFI1_HUMAN SFI1_HUMAN]] Plays a role in the dynamic structure of centrosome-associated contractile fibers via its interaction with CETN2.<ref>PMID:16956364</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Assairi, L]]		[[Category: Assairi, L]]
	[[Category: Blouquit, Y]]		[[Category: Blouquit, Y]]

OCA at 13:13, 16 January 2019

OCA — Wed, 16 Jan 2019 13:13:47 GMT

←Older revision		Revision as of 13:13, 16 January 2019
Line 3:		Line 3:
	<StructureSection load='2k2i' size='340' side='right' caption='[[2k2i]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>		<StructureSection load='2k2i' size='340' side='right' caption='[[2k2i]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2k2i]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K2I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2k2i]] is a 2 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=2K2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K2I FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [http://pdbe.org/2k2i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [http://www.ebi.ac.uk/pdbsum/2k2i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2i ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CETN2, CALT, CEN2 ([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=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [http://pdbe.org/2k2i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [http://www.ebi.ac.uk/pdbsum/2k2i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k2/2k2i_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k2/2k2i_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 31:		Line 32:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Assairi, L]]		[[Category: Assairi, L]]
	[[Category: Blouquit, Y]]		[[Category: Blouquit, Y]]
Line 40:		Line 42:
	[[Category: Cell division]]		[[Category: Cell division]]
	[[Category: Centrin 2]]		[[Category: Centrin 2]]
-	[[Category: Human]]
	[[Category: Mitosis]]		[[Category: Mitosis]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
	[[Category: Sfi1]]		[[Category: Sfi1]]

OCA at 12:10, 12 April 2017

OCA — Wed, 12 Apr 2017 12:10:03 GMT

←Older revision		Revision as of 12:10, 12 April 2017
Line 1:		Line 1:
		+
	==NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)==		==NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)==
	<StructureSection load='2k2i' size='340' side='right' caption='[[2k2i]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>		<StructureSection load='2k2i' size='340' side='right' caption='[[2k2i]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2k2i]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K2I FirstGlance]. <br>		<table><tr><td colspan='2'>[[2k2i]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K2I FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [http://www.ebi.ac.uk/pdbsum/2k2i PDBsum]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [http://pdbe.org/2k2i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [http://www.ebi.ac.uk/pdbsum/2k2i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k2i ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 25:		Line 26:
	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 2k2i" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:32, 1 July 2015

OCA — Wed, 01 Jul 2015 12:32:50 GMT

←Older revision		Revision as of 12:32, 1 July 2015
Line 2:		Line 2:
	<StructureSection load='2k2i' size='340' side='right' caption='[[2k2i]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>		<StructureSection load='2k2i' size='340' side='right' caption='[[2k2i]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2k2i]] is a 2 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=2K2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K2I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2k2i]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K2I FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CETN2, CALT, CEN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [http://www.ebi.ac.uk/pdbsum/2k2i 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=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [http://www.ebi.ac.uk/pdbsum/2k2i PDBsum]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
Line 30:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Homo sapiens]]
	[[Category: Assairi, L]]		[[Category: Assairi, L]]
	[[Category: Blouquit, Y]]		[[Category: Blouquit, Y]]

OCA at 13:50, 25 December 2014

OCA — Thu, 25 Dec 2014 13:50:59 GMT

←Older revision		Revision as of 13:50, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2k2i]] is a 2 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=2K2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K2I FirstGlance]. <br>		<table><tr><td colspan='2'>[[2k2i]] is a 2 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=2K2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K2I FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CETN2, CALT, CEN2 ([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">CETN2, CALT, CEN2 ([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>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [http://www.ebi.ac.uk/pdbsum/2k2i 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=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [http://www.ebi.ac.uk/pdbsum/2k2i PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CETN2_HUMAN CETN2_HUMAN]] Plays a fundamental role in microtubule-organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CEP110.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.<ref>PMID:8248209</ref> <ref>PMID:11279143</ref> <ref>PMID:12176356</ref> <ref>PMID:15964821</ref> <ref>PMID:17154534</ref> <ref>PMID:16760425</ref> [[http://www.uniprot.org/uniprot/SFI1_HUMAN SFI1_HUMAN]] Plays a role in the dynamic structure of centrosome-associated contractile fibers via its interaction with CETN2.<ref>PMID:16956364</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 29:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Assairi, L.]]	+	[[Category: Assairi, L]]
-	[[Category: Blouquit, Y.]]	+	[[Category: Blouquit, Y]]
-	[[Category: Craescu, C.]]	+	[[Category: Craescu, C]]
-	[[Category: Duchambon, P.]]	+	[[Category: Duchambon, P]]
-	[[Category: Martinez-Sanz, J.]]	+	[[Category: Martinez-Sanz, J]]
-	[[Category: Mouawad, L.]]	+	[[Category: Mouawad, L]]
	[[Category: Cell cycle]]		[[Category: Cell cycle]]
	[[Category: Cell division]]		[[Category: Cell division]]

OCA at 08:40, 30 September 2014

OCA — Tue, 30 Sep 2014 08:40:27 GMT

←Older revision		Revision as of 08:40, 30 September 2014
Line 1:		Line 1:
-	[[~~Image~~:2k2i.~~png\|left~~\|200px]]	+	==NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)==
		+	<StructureSection load='2k2i' size='340' side='right' caption='[[2k2i]], [[NMR_Ensembles_of_Models \| 15 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2k2i]] is a 2 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=2K2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K2I FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CETN2, CALT, CEN2 ([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>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k2i RCSB], [http://www.ebi.ac.uk/pdbsum/2k2i PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k2/2k2i_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Centrin, an EF-hand calcium-binding protein, has been shown to be involved in the duplication of centrosomes, and Sfi1 (Suppressor of fermentation-induced loss of stress resistance protein 1) is one of its centrosomal targets. There are three isoforms of human centrin, but here we only considered centrin 2 (HsCen2). This protein has the ability to bind to any of the approximately 25 repeats of human Sfi1 (hSfi1) with more or less affinity. In this study, we mainly focused on the 17th repeat (R17-hSfi1-20), which presents the highest level of similarity with a well-studied 17-residue peptide (P17-XPC) from human xeroderma pigmentosum complementation group C protein, another centrin target for DNA repair. The only known structure of HsCen2 was resolved in complex with P17-XPC. The 20-residue peptide R17-hSfi1-20 exhibits the motif L8L4W1, which is the reverse of the XPC motif, W1L4L8. Consequently, the dipole of the helix formed by this motif has a reverse orientation. We wished to ascertain the impact of this reversal on the structure, dynamics and affinity of centrin. To address this question, we determined the structure of C-HsCen2 [the C-terminal domain of HsCen2 (T94-Y172)] in complex with R17-hSfi1-20 and monitored its dynamics by NMR, after having verified that the N-terminal domain of HsCen2 does not interact with the peptide. The structure shows that the binding mode is similar to that of P17-XPC. However, we observed a 2 -A translation of the R17-hSfi1-20 helix along its axis, inducing less anchorage in the protein and the disruption of a hydrogen bond between a tryptophan residue in the peptide and a well-conserved nearby glutamate in C-HsCen2. NMR dynamic studies of the complex strongly suggested the existence of an unusual calcium secondary binding mode in calcium-binding loop III, made possible by the uncommon residue composition of this loop. The secondary metal site is only populated at high calcium concentration and depends on the type of bound ligand.

-	~~{{STRUCTURE_2k2i\| PDB=2k2i \| SCENE= }}~~	+	Structure, dynamics and thermodynamics of the human centrin 2/hSfi1 complex.,Martinez-Sanz J, Kateb F, Assairi L, Blouquit Y, Bodenhausen G, Abergel D, Mouawad L, Craescu CT J Mol Biol. 2010 Jan 8;395(1):191-204. Epub 2009 Oct 24. PMID:19857500<ref>PMID:19857500</ref>

-	~~===NMR Solution structure~~ of the ~~C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_19857500}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2k2i]] is a 2 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=2K2I OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:019857500<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Assairi, L.]]		[[Category: Assairi, L.]]

OCA: Protected "2k2i" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 13:39:18 GMT

Protected "2k2i" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:39, 7 January 2013

OCA at 13:39, 7 January 2013

OCA — Mon, 07 Jan 2013 13:39:15 GMT

←Older revision		Revision as of 13:39, 7 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2k2i.png\|left\|200px]]		[[Image:2k2i.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2k2i", 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_2k2i\| PDB=2k2i \| SCENE= }}		{{STRUCTURE_2k2i\| PDB=2k2i \| SCENE= }}

	===NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)===		===NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19857500}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19857500 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19857500}}		{{ABSTRACT_PUBMED_19857500}}

	==About this Structure==		==About this Structure==
-	~~2K2I~~ is a 2 ~~chains~~ structure ~~of sequences~~ 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=2K2I OCA].	+	[[2k2i]] is a 2 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=2K2I OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19857500~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019857500</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Assairi, L.]]		[[Category: Assairi, L.]]
Line 31:		Line 19:
	[[Category: Martinez-Sanz, J.]]		[[Category: Martinez-Sanz, J.]]
	[[Category: Mouawad, L.]]		[[Category: Mouawad, L.]]
-	[[Category: Calcium]]
	[[Category: Cell cycle]]		[[Category: Cell cycle]]
	[[Category: Cell division]]		[[Category: Cell division]]
Line 39:		Line 26:
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
	[[Category: Sfi1]]		[[Category: Sfi1]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Dec 24 07:34:36 2009''

OCA at 05:34, 24 December 2009

OCA — Thu, 24 Dec 2009 05:34:37 GMT

←Older revision		Revision as of 05:34, 24 December 2009
Line 12:		Line 12:
	===NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)===		===NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19857500}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19857500 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19857500}}

	==About this Structure==		==About this Structure==
Line 34:		Line 40:
	[[Category: Sfi1]]		[[Category: Sfi1]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed~~ Dec ~~23 09~~:08:27 2009''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Dec 24 07:34:36 2009''