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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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DOI no:
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Biochemistry
40:9596-9604
(2001)
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PubMed id:
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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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W.Schüler,
K.Kloiber,
T.Matt,
K.Bister,
R.Konrat.
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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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K.Loth,
D.Abergel,
P.Pelupessy,
M.Delarue,
P.Lopes,
J.Ouazzani,
N.Duclert-Savatier,
M.Nilges,
G.Bodenhausen,
and
V.Stoven
(2006).
Determination of dihedral Psi angles in large proteins by combining NH(N)/C(alpha)H(alpha) dipole/dipole cross-correlation and chemical shifts.
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Proteins,
64,
931-939.
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A.Velyvis,
J.Vaynberg,
Y.Yang,
O.Vinogradova,
Y.Zhang,
C.Wu,
and
J.Qin
(2003).
Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling.
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Nat Struct Biol,
10,
558-564.
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PDB code:
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J.E.Deane,
J.P.Mackay,
A.H.Kwan,
E.Y.Sum,
J.E.Visvader,
and
J.M.Matthews
(2003).
Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4.
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EMBO J,
22,
2224-2233.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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