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PDBsum entry 1m3v

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Metal binding protein PDB id
1m3v
Contents
Protein chain
122 a.a. *
Metals
_ZN ×2
* Residue conservation analysis

References listed in PDB file
Key reference
Title Structural basis for the recognition of ldb1 by the n-Terminal lim domains of lmo2 and lmo4.
Authors J.E.Deane, J.P.Mackay, A.H.Kwan, E.Y.Sum, J.E.Visvader, J.M.Matthews.
Ref. Embo J, 2003, 22, 2224-2233.
PubMed id 12727888
Abstract
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.
Secondary reference #1
Title 1h, 15n and 13c assignments of flin4, An intramolecular lmo4:ldb1 complex.
Authors J.E.Deane, J.E.Visvader, J.P.Mackay, J.M.Matthew.
Ref. J Biomol Nmr, 2002, 23, 165-166.
PubMed id 12153047
Abstract
Secondary reference #2
Title Design, Production and characterization of flin2 and flin4: the engineering of intramolecular ldb1:lmo complexes.
Authors J.E.Deane, E.Sum, J.P.Mackay, G.J.Lindeman, J.E.Visvader, J.M.Matthews.
Ref. Protein Eng, 2001, 14, 493-499.
PubMed id 11522923
Abstract
PROCHECK
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 Headers

 

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