1m3v

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(New page: 200px<br /><applet load="1m3v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3v" /> '''FLIN4: Fusion of the LIM binding domain of L...)
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[[Image:1m3v.jpg|left|200px]]<br /><applet load="1m3v" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m3v" />
caption="1m3v" />
'''FLIN4: Fusion of the LIM binding domain of Ldb1 and the N-terminal LIM domain of LMO4'''<br />
'''FLIN4: Fusion of the LIM binding domain of Ldb1 and the N-terminal LIM domain of LMO4'''<br />
==Overview==
==Overview==
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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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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.
==About this Structure==
==About this Structure==
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1M3V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M3V OCA].
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1M3V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3V OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Deane, J.E.]]
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[[Category: Deane, J E.]]
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[[Category: Kwan, A.H.Y.]]
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[[Category: Kwan, A H.Y.]]
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[[Category: Mackay, J.P.]]
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[[Category: Mackay, J P.]]
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[[Category: Matthews, J.M.]]
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[[Category: Matthews, J M.]]
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[[Category: Sum, E.Y.]]
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[[Category: Sum, E Y.]]
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[[Category: Visvader, J.E.]]
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[[Category: Visvader, J E.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: fusion protein]]
[[Category: fusion protein]]
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[[Category: lmo proteins]]
[[Category: lmo proteins]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:07:27 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:08 2008''

Revision as of 11:51, 21 February 2008


1m3v

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FLIN4: Fusion of the LIM binding domain of Ldb1 and the N-terminal LIM domain of LMO4

Overview

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.

About this Structure

1M3V is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4., Deane JE, Mackay JP, Kwan AH, Sum EY, Visvader JE, Matthews JM, EMBO J. 2003 May 1;22(9):2224-33. PMID:12727888

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