2f33: Difference between revisions
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==NMR solution structure of Ca2+-loaded calbindin D28K== | ==NMR solution structure of Ca2+-loaded calbindin D28K== | ||
<StructureSection load='2f33' size='340' side='right'caption='[[2f33 | <StructureSection load='2f33' size='340' side='right'caption='[[2f33]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2f33]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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=' | </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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Cavanagh J]] | ||
[[Category: | [[Category: Kojetin DJ]] | ||
[[Category: | [[Category: Kordys DR]] | ||
[[Category: | [[Category: Kumar R]] | ||
[[Category: | [[Category: Thompson RJ]] | ||
[[Category: | [[Category: Venters RA]] | ||
Latest revision as of 21:55, 29 May 2024
NMR solution structure of Ca2+-loaded calbindin D28KNMR solution structure of Ca2+-loaded calbindin D28K
Structural highlights
FunctionCALB1_RAT Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCalbindin-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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