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PDBsum entry 2e6w
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Metal binding protein
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PDB id
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2e6w
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References listed in PDB file
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Key reference
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Title
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Solution structure and calcium-Binding properties of ef-Hands 3 and 4 of calsenilin.
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Authors
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L.Yu,
C.Sun,
R.Mendoza,
J.Wang,
E.D.Matayoshi,
E.Hebert,
A.Pereda-Lopez,
P.J.Hajduk,
E.T.Olejniczak.
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Ref.
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Protein Sci, 2007,
16,
2502-2509.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 6.
Figure 6. Molecular surfaces of calsenilin EF3--4 colored by local
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Figure 7.
Figure 7. Ribbon plots comparing the structures of calsenilin EF3--4 (red)
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The above figures are
reprinted
by permission from the Protein Society:
Protein Sci
(2007,
16,
2502-2509)
copyright 2007.
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