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PDBsum entry 1qli
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Metal binding protein
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PDB id
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1qli
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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 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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Abstract
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Proteins of the cysteine-rich protein (CRP) family (CRP1, CRP2, and CRP3) are
implicated in diverse processes linked to cellular differentiation and growth
control. CRP proteins contain two LIM domains, each formed by two zinc-binding
modules of the CCHC and CCCC type, respectively. The solution structure of the
carboxyl-terminal LIM domain (LIM2) from recombinant quail CRP2 was determined
by multidimensional homo- and heteronuclear magnetic resonance spectroscopy. The
folding topology retains both independent zinc binding modules (CCHC and CCCC).
Each module consists of two orthogonally arranged antiparallel beta-sheets, and
the carboxyl-terminal CCCC module is terminated by an alpha-helix. 15N magnetic
relaxation data indicate that the modules differ in terms of conformational
flexibility. They pack together via a hydrophobic core region. In addition,
Arg122 in the CCHC module and Glu155 in the CCCC module are linked by an
intermodular hydrogen bond and/or salt bridge. These residues are absolutely
conserved in the CRP family of LIM proteins, and their interaction might
contribute to the relative orientation of the two zinc-binding modules in CRP
LIM2 domains. The global fold of quail CRP2 LIM2 is very similar to that of the
carboxyl-terminal LIM domain of the related but functionally distinct CRP family
member CRP1, analyzed recently. The carboxyl-terminal CCCC module is
structurally related to the DNA-binding domain of the erythroid transcription
factor GATA-1. In the two zinc-binding modules of quail CRP2 LIM2, flexible loop
regions made up of conserved amino acid residues are located on the same side of
the LIM2 domain and may cooperate in macromolecular recognition.
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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
reprinted
by permission from the ASBMB:
J Biol Chem
(1997,
272,
12001-12007)
copyright 1997.
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