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PDBsum entry 1m3v
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Metal binding protein
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PDB id
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1m3v
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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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Structural basis for the recognition of ldb1 by the n-Terminal lim domains of lmo2 and lmo4.
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Authors
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J.E.Deane,
J.P.Mackay,
A.H.Kwan,
E.Y.Sum,
J.E.Visvader,
J.M.Matthews.
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Ref.
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Embo J, 2003,
22,
2224-2233.
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PubMed id
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Abstract
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LMO2 and LMO4 are members of a small family of nuclear transcriptional
regulators that are important for both normal development and disease processes.
LMO2 is essential for hemopoiesis and angiogenesis, and inappropriate
overexpression of this protein leads to T-cell leukemias. LMO4 is
developmentally regulated in the mammary gland and has been implicated in breast
oncogenesis. Both proteins comprise two tandemly repeated LIM domains. LMO2 and
LMO4 interact with the ubiquitous nuclear adaptor protein ldb1/NLI/CLIM2, which
associates with the LIM domains of LMO and LIM homeodomain proteins via its LIM
interaction domain (ldb1-LID). We report the solution structures of two LMO:ldb1
complexes (PDB: 1M3V and 1J2O) and show that ldb1-LID binds to the N-terminal
LIM domain (LIM1) of LMO2 and LMO4 in an extended conformation, contributing a
third strand to a beta-hairpin in LIM1 domains. These findings constitute the
first molecular definition of LIM-mediated protein-protein interactions and
suggest a mechanism by which ldb1 can bind a variety of LIM domains that share
low sequence homology.
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Secondary reference #1
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Title
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1h, 15n and 13c assignments of flin4, An intramolecular lmo4:ldb1 complex.
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Authors
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J.E.Deane,
J.E.Visvader,
J.P.Mackay,
J.M.Matthew.
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Ref.
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J Biomol Nmr, 2002,
23,
165-166.
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PubMed id
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Secondary reference #2
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Title
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Design, Production and characterization of flin2 and flin4: the engineering of intramolecular ldb1:lmo complexes.
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Authors
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J.E.Deane,
E.Sum,
J.P.Mackay,
G.J.Lindeman,
J.E.Visvader,
J.M.Matthews.
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Ref.
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Protein Eng, 2001,
14,
493-499.
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PubMed id
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