2ami

<StructureSection load='2ami' size='340' side='right'caption='[[2ami]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2ami]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2AMI FirstGlance]. <br>

</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=2ami FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ami OCA], [https://pdbe.org/2ami PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ami RCSB], [https://www.ebi.ac.uk/pdbsum/2ami PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ami ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/CATR_CHLRE CATR_CHLRE]] This calcium-binding protein is found in the basal body complexes (the functional homolog of the centrosome in animal cell). In mitotic cells it is specifically associated with the poles of the mitotic spindles at the sites of the duplicated basal body complexes.

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Chlre]]

[[Category: Bunick, C G]]

[[Category: Chazin, W J]]

[[Category: Fagan, P A]]

[[Category: Hu, H T]]

[[Category: Sheehan, J H]]

[[Category: Four-helix bundle]]