View source for 1erc


==THE NMR SOLUTION STRUCTURE OF THE PHEROMONE ER-1 FROM THE CILIATED PROTOZOAN EUPLOTES RAIKOVI==
<StructureSection load='1erc' size='340' side='right'caption='[[1erc]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1erc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Euplotes_raikovi Euplotes raikovi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ERC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erc OCA], [https://pdbe.org/1erc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1erc RCSB], [https://www.ebi.ac.uk/pdbsum/1erc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1erc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MER1_EUPRA MER1_EUPRA] Mating ciliate pheromones (or gamones) are diffusible extracellular communication signals that distinguish different intraspecific classes of cells commonly referred to as 'mating types'. They prepare the latter for conjugation by changing their cell surface properties. The membrane-bound form promotes inter-cellular communication and adhesion for mating pair formation and may act as binding site for the secreted form.
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== Publication Abstract from PubMed ==
The 3-dimensional structure of the pheromone Er-1 isolated from the ciliated protozoan Euplotes raikovi has been determined in aqueous solution by 1H NMR spectroscopy. The structure of this 40-residue protein was calculated with the distance geometry program DIANA on the basis of 503 upper distance constraints derived from nuclear Overhauser effects and 77 dihedral angle constraints derived from spin-spin coupling constants, and refined by restrained energy minimization with the program OPAL. The Er-1 solution structure is represented by a group of 20 conformers with an average RMS deviation relative to the mean structure of 0.55 A for the backbone atoms N, C alpha, and C', and 0.93 A for all heavy atoms of the complete polypeptide chain, residues 1-40. The molecular architecture is dominated by an up-down-up bundle of 3 alpha-helices formed by residues 2-9, 12-19, and 24-33. Although this core part coincides closely with the previously determined structure of the homologous pheromone Er-10, the C-terminal peptide segment adopts a novel conformation. This is of interest in view of previous suggestions, based on sequence comparisons, that this molecular region may be important for the different specificity of receptor recognition by different pheromones.

The NMR solution structure of the pheromone Er-1 from the ciliated protozoan Euplotes raikovi.,Mronga S, Luginbuhl P, Brown LR, Ortenzi C, Luporini P, Bradshaw RA, Wuthrich K Protein Sci. 1994 Sep;3(9):1527-36. PMID:7833812<ref>PMID:7833812</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1erc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Euplotes raikovi]]
[[Category: Large Structures]]
[[Category: Bradshaw RA]]
[[Category: Brown LR]]
[[Category: Luginbuhl P]]
[[Category: Luporini P]]
[[Category: Mronga S]]
[[Category: Ortenzi C]]
[[Category: Wuthrich K]]