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PDBsum entry 1ibi
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Metal binding protein
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PDB id
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1ibi
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Application of cross-Correlated nmr spin relaxation to the zinc-Finger protein crp2(lim2): evidence for collective motions in lim domains.
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Authors
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W.Schüler,
K.Kloiber,
T.Matt,
K.Bister,
R.Konrat.
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Ref.
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Biochemistry, 2001,
40,
9596-9604.
[DOI no: ]
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PubMed id
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Abstract
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The solution structure of quail CRP2(LIM2) was significantly improved by using
an increased number of NOE constraints obtained from a 13C,15N-labeled protein
sample and by applying a recently developed triple-resonance cross-correlated
relaxation experiment for the determination of the backbone dihedral angle psi.
Additionally, the relative orientation of the 15N(i)-1HN(i) dipole and the
13CO(i) CSA tensor, which is related to both backbone angles phi and psi, was
probed by nitrogen-carbonyl multiple-quantum relaxation and used as an
additional constraint for the refinement of the local geometry of the
metal-coordination sites in CRP2(LIM2). The backbone dynamics of residues
located in the folded part of CRP2(LIM2) have been characterized by
proton-detected 13C'(i-1)-15N(i) and 15N(i)-1HN(i) multiple-quantum relaxation,
respectively. We show that regions having cross-correlated time modulation of
backbone isotropic chemical shifts on the millisecond to microsecond time scale
correlate with residues that are structurally altered in the mutant protein
CRP2(LIM2)R122A (disruption of the CCHC zinc-finger stabilizing side-chain
hydrogen bond) and that these residues are part of an extended hydrogen-bonding
network connecting the two zinc-binding sites. This indicates the presence of
long-range collective motions in the two zinc-binding subdomains. The
conformational plasticity of the LIM domain may be of functional relevance for
this important protein recognition motif.
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Secondary reference #1
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Title
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Structure of cysteine- And glycine-Rich protein crp2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains.
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Authors
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R.Konrat,
B.Kräutler,
R.Weiskirchen,
K.Bister.
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Ref.
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J Biol Chem, 1998,
273,
23233-23240.
[DOI no: ]
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PubMed id
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Figure 7.
Fig. 7. Surface structures of the LIM domains in CRP2.
Front (A and B) and back (C and D) views of the surface
structures of the LIM1 (A and C) and LIM2 (B and D) domains are
shown, revealing the differential distributions of hydrophobic
residues and of the electrostatic surface potential within the
two domains. In the surface structures, hydrophobic residues are
shown in white, positively charged residues in blue, and
negatively charged residues in red. The electrostatic surface
potential was calculated using the program MOLMOL (65).
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Figure 8.
Fig. 8. Ribbon diagram of full-length quail cysteine- and
glycine-rich protein CRP2. The diagram of the solution structure
was produced with the program MOLMOL (65). From the 58-amino
acid linker region between the two autonomously folded LIM
domains, approximately 50 central residues are structurally
disordered in solution. The four zinc ions are shown as spheres.
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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Secondary reference #2
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Title
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Solution structure of the carboxyl-Terminal lim domain from quail cysteine-Rich protein crp2.
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Authors
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R.Konrat,
R.Weiskirchen,
B.Kräutler,
K.Bister.
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Ref.
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J Biol Chem, 1997,
272,
12001-12007.
[DOI no: ]
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PubMed id
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Figure 5.
Fig. 5. Solution structure of qCRP2(LIM2). Stereoview showing
the overlay of 15 final structures of qCRP2(LIM2) for the
central residues 118-174. All backbone heavy atoms (N, C[  ], and
C  ) are shown.
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Figure 7.
Fig. 7. Superposition of qCRP2(LIM2) with corresponding
residues of chicken CRP1(LIM2). A and B, comparison of the
folding of the amino-terminal CCHC (A) and the carboxyl-terminal
CCCC^ (B) module of qCRP2(LIM2) (shown in light blue) and
chicken CRP1(LIM2) (shown in gray) (20).
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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