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PDBsum entry 2b1u
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Metal binding protein
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PDB id
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2b1u
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References listed in PDB file
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Key reference
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Title
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A structural and dynamic characterization of the ef-Hand protein clsp.
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Authors
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E.Babini,
I.Bertini,
F.Capozzi,
E.Chirivino,
C.Luchinat.
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Ref.
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Structure, 2006,
14,
1029-1038.
[DOI no: ]
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PubMed id
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Abstract
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The structure and dynamics of human calmodulin-like skin protein (CLSP) have
been characterized by NMR spectroscopy. The mobility of CLSP has been found to
be different for the N-terminal and C-terminal domains. The isolated domains
were also expressed and analyzed. The structure of the isolated C-terminal
domain is presented. The N-terminal domain is characterized by four stable
helices, which experience large fluctuations. This is shown to be due to
mutations in the hydrophobic core. The overall N-terminal domain behavior is
similar both in the full-length protein and in the isolated domain. By
exploiting the capability of Tb3+ bound to CLSP to induce partial orientation of
the molecule in a magnetic field, restricted motion of one domain with respect
to the other was proved. By using NMR, ITC, and ESI-MS, the calcium and
magnesium binding properties were investigated. Finally, CLSP is framed into the
evolutionary scheme of the calmodulin-like family.
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Figure 3.
Figure 3. Relaxation Parameters
^15N relaxation
parameters of full-length CLSP measured at 500 MHz and 25°C.
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Figure 4.
Figure 4. Comparison of CaM Structure and CLSP Model
Space-filling representation of the experimental CaM N-terminal
domain structure (PDB:1CFC) and of the CLSP N-terminal domain
model. The model was generated by the program MODELLER (6v2)
with the N-terminal domain of CaM (PDB: 1CFC) as template. (A),
(B), and (C) refer to different orientations of the protein
structures.
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The above figures are
reprinted
by permission from Cell Press:
Structure
(2006,
14,
1029-1038)
copyright 2006.
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