2g9b
From Proteopedia
(New page: 200px<br /><applet load="2g9b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g9b" /> '''NMR solution structure of CA2+-loaded calbin...) |
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| - | [[Image:2g9b.gif|left|200px]]<br /><applet load="2g9b" size=" | + | [[Image:2g9b.gif|left|200px]]<br /><applet load="2g9b" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR solution structure of CA2+-loaded calbindin D28K'''<br /> | '''NMR solution structure of CA2+-loaded calbindin D28K'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Calbindin-D(28K) is a Ca2+-binding protein, performing roles as both a | + | 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== | ==About this Structure== | ||
| - | 2G9B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 2G9B is a [http://en.wikipedia.org/wiki/Single_protein 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=2G9B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cavanagh, J.]] | [[Category: Cavanagh, J.]] | ||
| - | [[Category: Kojetin, D | + | [[Category: Kojetin, D J.]] |
| - | [[Category: Kordys, D | + | [[Category: Kordys, D R.]] |
[[Category: Kumar, R.]] | [[Category: Kumar, R.]] | ||
| - | [[Category: Thompson, R | + | [[Category: Thompson, R J.]] |
| - | [[Category: Venters, R | + | [[Category: Venters, R A.]] |
[[Category: ca2+-binding]] | [[Category: ca2+-binding]] | ||
[[Category: ef-hand]] | [[Category: ef-hand]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:29:28 2008'' |
Revision as of 15:29, 21 February 2008
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NMR solution structure of CA2+-loaded calbindin D28K
Overview
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
2G9B is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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
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