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データを開く
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基本情報
登録情報 | データベース: SASBDB / ID: SASDDQ4 |
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![]() | LIM/homeobox protein Lhx4 LIM domains fused to the LIM interaction domain (LID) of Insulin gene enhancer protein ISL-2
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機能・相同性 | ![]() visceral motor neuron differentiation / medial motor column neuron differentiation / spinal cord motor neuron cell fate specification / neuron fate specification / neuron fate commitment / methyl-CpG binding / motor neuron axon guidance / retinal ganglion cell axon guidance / negative regulation of neuron differentiation / cis-regulatory region sequence-specific DNA binding ...visceral motor neuron differentiation / medial motor column neuron differentiation / spinal cord motor neuron cell fate specification / neuron fate specification / neuron fate commitment / methyl-CpG binding / motor neuron axon guidance / retinal ganglion cell axon guidance / negative regulation of neuron differentiation / cis-regulatory region sequence-specific DNA binding / axonogenesis / RNA polymerase II transcription regulatory region sequence-specific DNA binding / animal organ morphogenesis / placenta development / neuron differentiation / DNA-binding transcription activator activity, RNA polymerase II-specific / DNA-binding transcription factor activity, RNA polymerase II-specific / apoptotic process / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleoplasm / nucleus / metal ion binding 類似検索 - 分子機能 |
生物種 | ![]() ![]() |
![]() | ![]() タイトル: Mutation in a flexible linker modulates binding affinity for modular complexes. 著者: Philippa H Stokes / Neil O Robertson / Ana P G Silva / Tanya Estephan / Jill Trewhella / J Mitchell Guss / Jacqueline M Matthews / ![]() 要旨: Tandem beta zippers are modular complexes formed between repeated linear motifs and tandemly arrayed domains of partner proteins in which β-strands form upon binding. Studies of such complexes, ...Tandem beta zippers are modular complexes formed between repeated linear motifs and tandemly arrayed domains of partner proteins in which β-strands form upon binding. Studies of such complexes, formed by LIM domain proteins and linear motifs in their intrinsically disordered partners, revealed spacer regions between the linear motifs that are relatively flexible but may affect the overall orientation of the binding modules. We demonstrate that mutation of a solvent exposed side chain in the spacer region of an LHX4-ISL2 complex has no significant effect on the structure of the complex, but decreases binding affinity, apparently by increasing flexibility of the linker. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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-モデル
モデル #1525 | ![]() タイプ: dummy / ダミー原子の半径: 2.00 A / 対称性: None コメント: One of 20 models generated using DAMMIN that went into creating the Damfilt model. カイ2乗値: 2.715 ![]() |
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モデル #1526 | ![]() タイプ: dummy / ダミー原子の半径: 2.00 A コメント: Damfilt model derived from multiple DAMMIN runs where 20 models were generated, spatially aligned. カイ2乗値: 2.715 ![]() |
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試料
![]() | 名称: LIM/homeobox protein Lhx4 LIM domains fused to the LIM interaction domain (LID) of Insulin gene enhancer protein ISL-2 試料濃度: 0.12-1.90 / Entity id: 814 / 815 |
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バッファ | 名称: 20 mM Tris, 150 mM NaCl, 1 mM TCEP / pH: 8 |
要素 #814 | 名称: Lhx4-LIM domains / タイプ: protein / 記述: LIM/homeobox protein Lhx4 / 分子量: 14.712 / 分子数: 1 / 由来: Mus musculus / 参照: UniProt: P53776 配列: GSMQQIPQCA GCNQHILDKF ILKVLDRHWH SSCLKCADCQ MQLADRCFSR AGSVYCKEDF FKRFGTKCTA CQQGIPPTQV VRKAQDFVYH LHCFACIICN RQLATGDEFY LMEDGRLVCK EDYETAKQ |
要素 #815 | 名称: ISL-2 / タイプ: protein / 記述: Insulin gene enhancer protein ISL-2 / 分子量: 4.031 / 分子数: 1 / 由来: Mus musculus / 参照: UniProt: Q9CXV0 配列: GGSGGHMGSG GGTPLVAGSP IRHENAVQGS AVEVQTYQPP W |
-実験情報
ビーム | 設備名称: Australian Synchrotron SAXS/WAXS / 地域: Melbourne / 国: Australia ![]() | ||||||||||||||||||||||||||||||||||||
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検出器 | 名称: Pilatus 1M / タイプ: Dectris / Pixsize x: 172 mm | ||||||||||||||||||||||||||||||||||||
スキャン | 測定日: 2015年11月19日 / セル温度: 13.5 °C / 照射時間: 1 sec. / フレーム数: 24 / 単位: 1/A /
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距離分布関数 P(R) |
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結果 | コメント: The protein analysed consists of a fusion of two interacting partner proteins: the LIM domains of Lhx4 and the LID of Isl2. The ab initio bead models presented in this entry include: 1) ...コメント: The protein analysed consists of a fusion of two interacting partner proteins: the LIM domains of Lhx4 and the LID of Isl2. The ab initio bead models presented in this entry include: 1) The best-fit individual reconstruction (top) and; 2) The spatially aligned and volume/bead occupancy-corrected averaged representation of the protein in solution (bottom) calculated from twenty individual reconstructions (NSD = 0.68; resolution estimate = 2.8 nm). Five concentrations of protein were subjected to SAXS as static samples (96-well plate) at the Australian Synchrotron. Subtle concentration dependent effects were noted. All data and additional information relating to the concentration series is included in the full-entry zip archive. The protein was subjected to SEC (off line) as the last purification step just prior to data collection. Also refer to the related SASBDB entry SASDDR4.
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