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Contents |
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* Residue conservation analysis
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PDB id:
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Contractile
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Title:
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Solution structure of the chicken crp1
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Structure:
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Protein (crp1). Chain: a. Fragment: lim-domain protein. Engineered: yes
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Source:
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Gallus gallus. Chicken. Organism_taxid: 9031. Tissue: muscle. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: bl21(de3).
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NMR struc:
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37 models
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Authors:
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X.Yao,G.C.Perez-Alvarado,H.A.Louis,P.Pomies,C.Hatt, M.F.Summers,M.C.Beckerle
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Key ref:
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X.Yao
et al.
(1999).
Solution structure of the chicken cysteine-rich protein, CRP1, a double-LIM protein implicated in muscle differentiation.
Biochemistry,
38,
5701-5713.
PubMed id:
DOI:
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Date:
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02-Feb-99
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Release date:
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06-May-99
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PROCHECK
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Headers
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References
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P67966
(CSRP1_CHICK) -
Cysteine and glycine-rich protein 1
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Seq:
Struc:
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192 a.a.
192 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Gene Ontology (GO) functional annotation
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Cellular component
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cytoplasm
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2 terms
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Biochemical function
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protein binding
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3 terms
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DOI no:
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Biochemistry
38:5701-5713
(1999)
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PubMed id:
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Solution structure of the chicken cysteine-rich protein, CRP1, a double-LIM protein implicated in muscle differentiation.
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X.Yao,
G.C.Pérez-Alvarado,
H.A.Louis,
P.Pomiès,
C.Hatt,
M.F.Summers,
M.C.Beckerle.
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ABSTRACT
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The mechanism by which the contractile machinery of muscle is assembled and
maintained is not well-understood. Members of the cysteine-rich protein (CRP)
family have been implicated in these processes. Three vertebrate CRPs (CRP1-3)
that exhibit developmentally regulated muscle-specific expression have been
identified. All three proteins are associated with the actin cytoskeleton, and
one has been shown to be required for striated muscle structure and function.
The vertebrate CRPs identified to date display a similar molecular architecture;
each protein is comprised of two tandemly arrayed LIM domains, protein-binding
motifs found in a number of proteins with roles in cell differentiation. Each
LIM domain coordinates two Zn(II) ions that are bound independently in CCHC
(C=Cys, H=His) and CCCC modules. Here we describe the solution structure of
chicken CRP1 determined by homonuclear and 1H-15N heteronuclear magnetic
resonance spectroscopy. Comparison of the structures of the two LIM domains of
CRP1 reveals a high degree of similarity in their tertiary folds. In addition,
the two component LIM domains represent two completely independent folding units
and exhibit no apparent interactions with each other. The structural
independence and spatial separation of the two LIM domains of CRP1 are
compatible with an adapter or linker role for the protein.
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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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J.F.Sagave,
M.Moser,
E.Ehler,
S.Weiskirchen,
D.Stoll,
K.Günther,
R.Büttner,
and
R.Weiskirchen
(2008).
Targeted disruption of the mouse Csrp2 gene encoding the cysteine- and glycine-rich LIM domain protein CRP2 result in subtle alteration of cardiac ultrastructure.
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BMC Dev Biol, 8,
80.
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C.Thomas,
F.Moreau,
M.Dieterle,
C.Hoffmann,
S.Gatti,
C.Hofmann,
M.Van Troys,
C.Ampe,
and
A.Steinmetz
(2007).
The LIM domains of WLIM1 define a new class of actin bundling modules.
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J Biol Chem, 282,
33599-33608.
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T.Zhang,
S.Zhuang,
D.E.Casteel,
D.J.Looney,
G.R.Boss,
and
R.B.Pilz
(2007).
A cysteine-rich LIM-only protein mediates regulation of smooth muscle-specific gene expression by cGMP-dependent protein kinase.
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J Biol Chem, 282,
33367-33380.
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B.J.Martinsen,
A.N.Neumann,
A.J.Frasier,
C.V.Baker,
C.E.Krull,
and
J.L.Lohr
(2006).
PINCH-1 expression during early avian embryogenesis: implications for neural crest and heart development.
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Dev Dyn, 235,
152-162.
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J.Wang,
C.Y.Deng,
Y.Z.Xiong,
B.Zuo,
L.Xing,
F.E.Li,
M.G.Lei,
R.Zheng,
and
S.W.Jiang
(2005).
cDNA cloning, sequence analysis of the porcine LIM and cysteine-rich domain 1 gene.
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Acta Biochim Biophys Sin (Shanghai), 37,
843-850.
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A.Casrouge,
R.Veitia,
J.Kirchner,
M.J.Bevan,
and
J.Kanellopoulos
(2004).
The human and mouse orthologous LIM-only proteins respectively encoded in chromosome 6 and 17 show a different expression pattern.
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Microbes Infect, 6,
1063-1072.
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J.L.Kadrmas,
and
M.C.Beckerle
(2004).
The LIM domain: from the cytoskeleton to the nucleus.
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Nat Rev Mol Cell Biol, 5,
920-931.
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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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W.M.Campana,
R.R.Myers,
and
A.Rearden
(2003).
Identification of PINCH in Schwann cells and DRG neurons: shuttling and signaling after nerve injury.
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Glia, 41,
213-223.
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C.A.Blindauer,
M.D.Harrison,
A.K.Robinson,
J.A.Parkinson,
P.W.Bowness,
P.J.Sadler,
and
N.J.Robinson
(2002).
Multiple bacteria encode metallothioneins and SmtA-like zinc fingers.
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Mol Microbiol, 45,
1421-1432.
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C.A.Blindauer,
M.D.Harrison,
J.A.Parkinson,
A.K.Robinson,
J.S.Cavet,
N.J.Robinson,
and
P.J.Sadler
(2001).
A metallothionein containing a zinc finger within a four-metal cluster protects a bacterium from zinc toxicity.
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Proc Natl Acad Sci U S A, 98,
9593-9598.
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PDB code:
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N.V.Grishin
(2001).
Treble clef finger--a functionally diverse zinc-binding structural motif.
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Nucleic Acids Res, 29,
1703-1714.
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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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Links
