This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2f33
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2f33" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f33" /> '''NMR solution structure of Ca2+-loaded calbin...) |
|||
| (13 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2f33.gif|left|200px]]<br /><applet load="2f33" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2f33" /> | ||
| - | '''NMR solution structure of Ca2+-loaded calbindin D28K'''<br /> | ||
| - | == | + | ==NMR solution structure of Ca2+-loaded calbindin D28K== |
| - | Calbindin-D(28K) is a Ca2+-binding protein, performing roles as both a | + | <StructureSection load='2f33' size='340' side='right'caption='[[2f33]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2f33]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F33 FirstGlance]. <br> | ||
| + | </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=2f33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f33 OCA], [https://pdbe.org/2f33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f33 RCSB], [https://www.ebi.ac.uk/pdbsum/2f33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f33 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CALB1_RAT CALB1_RAT] Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. | ||
| + | == 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/f3/2f33_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/main_output.php?pdb_ID=2f33 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Calbindin-D(28K) is a Ca2+-binding protein, performing roles as both a calcium buffer and calcium sensor. The NMR solution structure of Ca2+-loaded calbindin-D(28K) reveals a single, globular fold consisting of six distinct EF-hand subdomains, which coordinate Ca2+ in loops on EF1, EF3, EF4 and EF5. Target peptides from Ran-binding protein M and myo-inositol monophosphatase, along with a new target from procaspase-3, are shown to interact with the protein on a surface comprised of alpha5 (EF3), alpha8 (EF4) and the EF2-EF3 and EF4-EF5 loops. Fluorescence experiments reveal that calbindin-D(28K) adopts discrete hydrophobic states as it binds Ca2+. The structure, binding interface and hydrophobic characteristics of Ca2+-loaded calbindin-D(28K) provide the first detailed insights into how this essential protein may function. This structure is one of the largest high-resolution NMR structures and the largest monomeric EF-hand protein to be solved to date. | ||
| - | + | Structure, binding interface and hydrophobic transitions of Ca2+-loaded calbindin-D(28K).,Kojetin DJ, Venters RA, Kordys DR, Thompson RJ, Kumar R, Cavanagh J Nat Struct Mol Biol. 2006 Jul;13(7):641-7. Epub 2006 Jun 25. PMID:16799559<ref>PMID:16799559</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2f33" style="background-color:#fffaf0;"></div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ==See Also== | |
| + | *[[S100 proteins 3D structures|S100 proteins 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rattus norvegicus]] | ||
| + | [[Category: Cavanagh J]] | ||
| + | [[Category: Kojetin DJ]] | ||
| + | [[Category: Kordys DR]] | ||
| + | [[Category: Kumar R]] | ||
| + | [[Category: Thompson RJ]] | ||
| + | [[Category: Venters RA]] | ||
Current revision
NMR solution structure of Ca2+-loaded calbindin D28K
| |||||||||||

