Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.
about
The structural basis of integrin-linked kinase-PINCH interactionsMolecular recognition of the Tes LIM2-3 domains by the actin-related protein Arp7AStabilization of a binary protein complex by intein-mediated cyclizationStructures of three members of Pfam PF02663 (FmdE) implicated in microbial methanogenesis reveal a conserved α+β core domain and an auxiliary C-terminal treble-clef zinc fingerImplementing the LIM code: the structural basis for cell type-specific assembly of LIM-homeodomain complexesSolution structure of the U2 snRNP protein Rds3p reveals a knotted zinc-finger motifCrystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domainsStructural and Functional Analysis of the Tandem -Zipper Interaction of a Streptococcal Protein with Human FibronectinStructural basis of simultaneous recruitment of the transcriptional regulators LMO2 and FOG1/ZFPM1 by the transcription factor GATA1Solution structure of a tethered Lmo2LIM2/Ldb1LIDcomplexStructural Basis for Partial Redundancy in a Class of Transcription Factors, the LIM Homeodomain Proteins, in Neural Cell Type SpecificationA Structural Basis for the Regulation of the LIM-Homeodomain Protein Islet 1 (Isl1) by Intra- and Intermolecular InteractionsConformational flexibility of the oncogenic protein LMO2 primes the formation of the multi-protein transcription complexThe tandem β-zipper: modular binding of tandem domains and linear motifs.Interactions between LHX3- and ISL1-family LIM-homeodomain transcription factors are conserved in Caenorhabditis elegansThe co-factor of LIM domains (CLIM/LDB/NLI) maintains basal mammary epithelial stem cells and promotes breast tumorigenesis.Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.Solution structure of the LIM-homeodomain transcription factor complex Lhx3/Ldb1 and the effects of a pituitary mutation on key Lhx3 interactionsThe diverse biofunctions of LIM domain proteins: determined by subcellular localization and protein-protein interaction.The structure of an LIM-only protein 4 (LMO4) and Deformed epidermal autoregulatory factor-1 (DEAF1) complex reveals a common mode of binding to LMO4.Exome sequencing identifies a missense mutation in Isl1 associated with low penetrance otitis media in dearisch miceFusion-protein-assisted protein crystallizationIn silico design of a DNA-based HIV-1 multi-epitope vaccine for Chinese populations.Crystallization and diffraction of an Isl1-Ldb1 complex.Linkers in the structural biology of protein-protein interactionsDrosophila LIM-only is a positive regulator of transcription during thoracic bristle development.LIM-domain-only proteins in cancer.The role of chromatin remodeling in medulloblastoma.LIM-domain-only proteins: multifunctional nuclear transcription coregulators that interacts with diverse proteins.The LIM-only factor LMO4 regulates expression of the BMP7 gene through an HDAC2-dependent mechanism, and controls cell proliferation and apoptosis of mammary epithelial cells.The promises and challenges of fusion constructs in protein biochemistry and enzymology.Induction of multiple cytotoxic T lymphocyte responses in mice by a multiepitope DNA vaccine against dengue virus serotype 1.A Quantitative Fluorescence-Based Assay for Assessing LIM Domain-Peptide Interactions.LMO4 functions as a co-activator of neurogenin 2 in the developing cortex.Purification, crystallization and preliminary X-ray analysis of a fusion of the LIM domains of LMO2 and the LID domain of Ldb1.Crystallization and diffraction of an Lhx4-Isl2 complex.A regulatory network to segregate the identity of neuronal subtypes.Targeting LMO2 with a peptide aptamer establishes a necessary function in overt T-cell neoplasia.¹H, ¹⁵N and ¹³C assignments of an intramolecular LMO4-LIM1/CtIP complex.Disparate binding kinetics by an intrinsically disordered domain enables temporal regulation of transcriptional complex formation.
P2860
Q24324678-502BF5B5-88BF-49F5-AE53-A709376F2743Q24338679-08430C5A-A95F-4B2E-9337-0A58C62C57D9Q24648142-7D101619-C156-4DC6-9082-04F0C7A0AEACQ27644457-7C21825F-521C-47F5-8B33-7918C08A461DQ27650961-08801289-E6E9-4FBC-8228-CD53784BF28AQ27651175-EBF2CD27-EDC7-4A2F-99AF-DDA2C7B18E96Q27651687-CDC0650E-84A1-495E-AB40-6678B5E702EBQ27671736-0CEA9DE0-4DE8-47D1-95E9-1B36795EBBA3Q27671779-EF79AD1A-3096-4C28-A2DC-1C3D35DCFA5FQ27671803-4CDD6ECD-54AC-479F-BB19-EFA67FC1F21DQ27675210-03300340-53AA-42E8-A195-9DF97E194E67Q27678554-12A8D1BE-CDA6-4F78-B249-11B90B426FEFQ27681258-A3F6E3FF-BE1C-4D9B-8988-943D6F21CF9AQ27691999-72CDB6DD-749A-4158-89E4-7A96841F3306Q33870828-6A3B8EFC-74FC-4CB9-B1EE-60BDA47E5270Q33981658-60AD558D-5985-4341-93C3-93D9D3C910AAQ34314302-1671D9F1-848C-42BB-8FCA-2BB10CEC5570Q34358031-E51C90D1-01A8-4916-B557-9CCBC9268645Q34662765-0E1F911D-647F-4FE2-AA9C-87AD8CEC24AFQ35326762-D36616B3-3A4D-4EA3-A728-19408FB814F2Q35840689-38E6E28A-8A65-4FEE-9F1D-8BBD8BB9AEFAQ35841518-488C5C91-5C36-45A5-9102-0B5E491DDD6DQ35887235-29E4ED2C-DC68-44E0-8D8D-8677F5744F06Q36448244-CD2FD1D5-D1AF-4426-B973-196ED0F507FFQ36658560-0B8CC808-64AF-4E44-91F2-7691D86F999FQ36837038-91ED3A87-19A9-434D-A437-116B0E558A22Q38072838-BEBC67A0-D09C-4E86-9C1E-2E383EE27623Q38083796-97762C44-7ED0-45E3-9231-B03097B6CD38Q38174833-C221DC86-D817-4F84-9FDF-7EBF4C15E15EQ38302448-73DF2088-C4BC-4049-90B3-57B7A99E7C08Q38829746-991F64C3-454D-4D4B-9C5A-3EAC3B16F736Q38942473-CC3A7FCD-10A6-41C6-B977-29602BAB9ED0Q39372345-794B0384-A813-4A91-B06A-D497E9A738F3Q39528858-BB41F895-90B5-4270-9B6B-83FBC5423BEEQ41147197-C6B8FAA2-6221-4EC3-A777-DC2DF3551A4FQ41783790-48D4E3DC-800F-48E0-8679-7960CE1306D2Q41853998-6E2866FC-BB6C-4425-949F-468CC51E7ACBQ42124810-5932328E-322F-40FE-9569-3D6F9FAA1040Q46052816-8A35EC41-6051-4CA1-BC8C-80702D7AD2F9Q52318671-0AE22460-5E36-4365-98E1-6288716273D2
P2860
Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.
@en
type
label
Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.
@en
prefLabel
Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.
@en
P2860
P50
P356
P1433
P1476
Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.
@en
P2093
J Mitchell Guss
Jane E Visvader
P2860
P304
P356
10.1038/SJ.EMBOJ.7600376
P407
P577
2004-09-02T00:00:00Z