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[[Image:2f33.gif|left|200px]]
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{{STRUCTURE_2f33|  PDB=2f33  |  SCENE=  }}
'''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]]' 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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2F33 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F33 OCA].
</div>
<div class="pdbe-citations 2f33" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/16799559 16799559]
*[[S100 proteins 3D structures|S100 proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Cavanagh J]]
[[Category: Cavanagh, J.]]
[[Category: Kojetin DJ]]
[[Category: Kojetin, D J.]]
[[Category: Kordys DR]]
[[Category: Kordys, D R.]]
[[Category: Kumar R]]
[[Category: Kumar, R.]]
[[Category: Thompson RJ]]
[[Category: Thompson, R J.]]
[[Category: Venters RA]]
[[Category: Venters, R A.]]
[[Category: Ca2+-binding]]
[[Category: Ef-hand]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:24:25 2008''

Latest revision as of 18:55, 29 May 2024

NMR solution structure of Ca2+-loaded calbindin D28K

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