2ami
From Proteopedia
(Difference between revisions)
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- | + | ==Solution Structure Of The Calcium-loaded N-Terminal Sensor Domain Of Centrin== | |
- | + | <StructureSection load='2ami' size='340' side='right' caption='[[2ami]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[2ami]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AMI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AMI FirstGlance]. <br> | ||
+ | </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=2ami FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ami OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ami RCSB], [http://www.ebi.ac.uk/pdbsum/2ami 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/am/2ami_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 is an essential component of microtubule-organizing centers in organisms ranging from algae and yeast to humans. It is an EF-hand calcium-binding protein with homology to calmodulin but distinct calcium binding properties. In a previously proposed model, the C-terminal domain of centrin serves as a constitutive anchor to target proteins, and the N-terminal domain serves as the sensor of calcium signals. The three-dimensional structure of the N-terminal domain of Chlamydomonas rheinhardtii centrin has been determined in the presence of calcium by solution NMR spectroscopy. The domain is found to occupy an open conformation typical of EF-hand calcium sensors. Comparison of the N- and C-terminal domains of centrin reveals a structural and biochemical basis for the domain specificity of interactions with its cellular targets and the distinct nature of centrin relative to other EF-hand proteins. An NMR titration of the centrin N-terminal domain with a fragment of the known centrin target Sfi1 reveals binding of the peptide to a discrete site on the protein, which supports the proposal that the N-terminal domain serves as a calcium sensor in centrin. | ||
- | + | Structure of the N-terminal calcium sensor domain of centrin reveals the biochemical basis for domain-specific function.,Sheehan JH, Bunick CG, Hu H, Fagan PA, Meyn SM, Chazin WJ J Biol Chem. 2006 Feb 3;281(5):2876-81. Epub 2005 Nov 29. PMID:16317001<ref>PMID:16317001</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Chlre]] | [[Category: Chlre]] | ||
[[Category: Bunick, C G.]] | [[Category: Bunick, C G.]] |
Revision as of 10:36, 3 October 2014
Solution Structure Of The Calcium-loaded N-Terminal Sensor Domain Of Centrin
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