2e6w
From Proteopedia
(New page: 200px<br /><applet load="2e6w" size="350" color="white" frame="true" align="right" spinBox="true" caption="2e6w" /> '''Solution structure and calcium binding prope...) |
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==Overview== | ==Overview== | ||
| - | Calsenilin is a member of the recoverin branch of the EF-hand superfamily | + | Calsenilin is a member of the recoverin branch of the EF-hand superfamily that is reported to interact with presenilins, regulate prodynorphin gene expression, modulate voltage-gated Kv4 potassium channel function, and bind to neurotoxins. Calsenilin is a Ca+2-binding protein and plays an important role in calcium signaling. Despite its importance in numerous neurological functions, the structure of this protein has not been reported. In the absence of Ca+2, the protein has limited spectral resolution that increases upon the addition of Ca+2. Here, we describe the three-dimensional solution structure of EF-hands 3 and 4 of calsenilin in the Ca+2-bound form. The Ca+2-bound structure consists of five alpha-helices and one two-stranded antiparallel beta-sheet. The long loop that connects EF hands 3 and 4 is highly disordered in solution. In addition to its structural effects, Ca+2 binding also increases the protein's propensity to dimerize. These changes in structure and oligomerization state induced upon Ca+2 binding may play important roles in molecular recognition during calcium signaling. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hajduk, P | + | [[Category: Hajduk, P J.]] |
[[Category: Hebert, E.]] | [[Category: Hebert, E.]] | ||
[[Category: Mendoza, R.]] | [[Category: Mendoza, R.]] | ||
| - | [[Category: Olejniczak, E | + | [[Category: Olejniczak, E T.]] |
[[Category: Pereda-Lopez, A.]] | [[Category: Pereda-Lopez, A.]] | ||
[[Category: Sun, C.]] | [[Category: Sun, C.]] | ||
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[[Category: metal binding protein]] | [[Category: metal binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:06:46 2008'' |
Revision as of 15:06, 21 February 2008
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Solution structure and calcium binding properties of EF-hands 3 and 4 of calsenilin
Overview
Calsenilin is a member of the recoverin branch of the EF-hand superfamily that is reported to interact with presenilins, regulate prodynorphin gene expression, modulate voltage-gated Kv4 potassium channel function, and bind to neurotoxins. Calsenilin is a Ca+2-binding protein and plays an important role in calcium signaling. Despite its importance in numerous neurological functions, the structure of this protein has not been reported. In the absence of Ca+2, the protein has limited spectral resolution that increases upon the addition of Ca+2. Here, we describe the three-dimensional solution structure of EF-hands 3 and 4 of calsenilin in the Ca+2-bound form. The Ca+2-bound structure consists of five alpha-helices and one two-stranded antiparallel beta-sheet. The long loop that connects EF hands 3 and 4 is highly disordered in solution. In addition to its structural effects, Ca+2 binding also increases the protein's propensity to dimerize. These changes in structure and oligomerization state induced upon Ca+2 binding may play important roles in molecular recognition during calcium signaling.
About this Structure
2E6W is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin., Yu L, Sun C, Mendoza R, Wang J, Matayoshi ED, Hebert E, Pereda-Lopez A, Hajduk PJ, Olejniczak ET, Protein Sci. 2007 Nov;16(11):2502-9. PMID:17962406
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