[English] 日本語
![](img/lk-miru.gif)
- SASDDQ4: LIM/homeobox protein Lhx4 LIM domains fused to the LIM interactio... -
+
Open data
-
Basic information
Entry | Database: SASBDB / ID: SASDDQ4 |
---|---|
![]() | LIM/homeobox protein Lhx4 LIM domains fused to the LIM interaction domain (LID) of Insulin gene enhancer protein ISL-2
|
Function / homology | ![]() 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 / ![]() ![]() ![]() ![]() Similarity search - Function |
Biological species | ![]() ![]() ![]() |
![]() | ![]() Title: Mutation in a flexible linker modulates binding affinity for modular complexes. Authors: Philippa H Stokes / Neil O Robertson / Ana P G Silva / Tanya Estephan / Jill Trewhella / J Mitchell Guss / Jacqueline M Matthews / ![]() Abstract: 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. |
![]() |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-Data source
SASBDB page | ![]() |
---|
-Related structure data
-
External links
Related items in Molecule of the Month |
---|
-Models
Model #1525 | ![]() Type: dummy / Radius of dummy atoms: 2.00 A / Symmetry ![]() Comment: One of 20 models generated using DAMMIN that went into creating the Damfilt model. Chi-square value: 2.715 ![]() |
---|---|
Model #1526 | ![]() Type: dummy / Radius of dummy atoms: 2.00 A Comment: Damfilt model derived from multiple DAMMIN runs where 20 models were generated, spatially aligned. Chi-square value: 2.715 ![]() |
-
Sample
![]() | Name: LIM/homeobox protein Lhx4 LIM domains fused to the LIM interaction domain (LID) of Insulin gene enhancer protein ISL-2 Specimen concentration: 0.12-1.90 / Entity id: 814 / 815 |
---|---|
Buffer | Name: 20 mM Tris, 150 mM NaCl, 1 mM TCEP / pH: 8 |
Entity #814 | Name: Lhx4-LIM domains / Type: protein / Description: LIM/homeobox protein Lhx4 / Formula weight: 14.712 / Num. of mol.: 1 / Source: Mus musculus / References: UniProt: P53776 Sequence: GSMQQIPQCA GCNQHILDKF ILKVLDRHWH SSCLKCADCQ MQLADRCFSR AGSVYCKEDF FKRFGTKCTA CQQGIPPTQV VRKAQDFVYH LHCFACIICN RQLATGDEFY LMEDGRLVCK EDYETAKQ |
Entity #815 | Name: ISL-2 / Type: protein / Description: Insulin gene enhancer protein ISL-2 / Formula weight: 4.031 / Num. of mol.: 1 / Source: Mus musculus / References: UniProt: Q9CXV0 Sequence: GGSGGHMGSG GGTPLVAGSP IRHENAVQGS AVEVQTYQPP W |
-Experimental information
Beam | Instrument name: Australian Synchrotron SAXS/WAXS / City: Melbourne / 国: Australia ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Detector | Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm | ||||||||||||||||||||||||||||||||||||
Scan | Measurement date: Nov 19, 2015 / Cell temperature: 13.5 °C / Exposure time: 1 sec. / Number of frames: 24 / Unit: 1/A /
| ||||||||||||||||||||||||||||||||||||
Distance distribution function P(R) |
| ||||||||||||||||||||||||||||||||||||
Result | Comments: 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 ...Comments: 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.
|