3MMK

The structural basis for partial redundancy in a class of transcription factors, the lim-homeodomain proteins, in neural cell type specification

3MMK の概要

• エントリーDOI: 10.2210/pdb3mmk/pdb
• 関連するPDBエントリー: 2RGT
• 分子名称: Fusion of LIM/homeobox protein Lhx4, linker, Insulin gene enhancer protein ISL-2, ZINC ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: protein-protein complex, lim domain, zn finger, dna-binding, homeobox, metal-binding, nucleus, transcription, transcriptional regulation, metal binding protein
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Nucleus : Q9CXV0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37963.61

構造登録者

Gadd, M.S.,Langley, D.B.,Guss, J.M.,Matthews, J.M. (登録日: 2010-04-20, 公開日: 2011-07-13, 最終更新日: 2024-03-20)

主引用文献

Gadd, M.S.,Bhati, M.,Jeffries, C.M.,Langley, D.B.,Trewhella, J.,Guss, J.M.,Matthews, J.M.
The structural basis for partial redundancy in a class of transcription factors, the lim-homeodomain proteins, in neural cell type specification.
J.Biol.Chem., 2011

PubMed Abstract: Combinations of LIM homeodomain proteins form a transcriptional "LIM code" to direct the specification of neural cell types. Two paralogous pairs of LIM homeodomain proteins, LIM homeobox protein 3/4 (Lhx3/Lhx4) and Islet-1/2 (Isl1/Isl2), are expressed in developing ventral motor neurons. Lhx3 and Isl1 interact within a well characterized transcriptional complex that triggers motor neuron development, but it was not known whether Lhx4 and Isl2 could participate in equivalent complexes. We have identified an Lhx3-binding domain (LBD) in Isl2 based on sequence homology with the Isl1(LBD) and show that both Isl2(LBD) and Isl1(LBD) can bind each of Lhx3 and Lhx4. X-ray crystal- and small-angle x-ray scattering-derived solution structures of an Lhx4·Isl2 complex exhibit many similarities with that of Lhx3·Isl1; however, structural differences supported by mutagenic studies reveal differences in the mechanisms of binding. Differences in binding have implications for the mode of exchange of protein partners in transcriptional complexes and indicate a divergence in functions of Lhx3/4 and Isl1/2. The formation of weaker Lhx·Isl complexes would likely be masked by the availability of the other Lhx·Isl complexes in postmitotic motor neurons.

PubMed: 22025611
DOI: 10.1074/jbc.M111.248559

実験手法

X-RAY DIFFRACTION (2.157 Å)