2k2i

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
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]]

Revision as of 08:06, 7 April 2021

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)

PDB ID 2k2i

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k2i"
Personal tools