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  • subunit
  • Like other voltage-gated potassium channels, KCNH channels are tetrameric, and each subunit has six transmembrane domains, a pore-loop domain, and intracellular amino and carboxy termini ( Warmke and Ganetzky, 1994 ). (rupress.org)
  • structural
  • A limited number of mutations in the C-terminal domain ( 12 ) or the linker region ( 13 ) affect repressor activity, but the structural nature of this regulation by the C-terminal domain has been obscure. (pnas.org)
  • A critical step in our approach is to use different templates of Ras complexes, in order to account for the structural variation among the RA and RB domains. (crg.eu)
  • According to structural analyses [( PUBMED:9302998 ), ( PUBMED:10369774 ), ( PUBMED:11160884 )], the KH domain can be separated in two groups - type 1 and type 2. (embl-heidelberg.de)
  • residues
  • Additionally, a channel bearing a group of eight alanine residues in the S4-S5 linker was not measurably regulated by N-eag-CFP domains, but robust FRET was measured. (rupress.org)
  • The solution structure of the C-terminal domain, consisting of residues N130-L226 plus a 13-residue N-terminal extension, has been determined by using NMR spectroscopy. (pnas.org)
  • Residues before A147 are highly mobile and adopt a random coil conformation, but residues A147-L226 form a single structured domain consisting of five β-strands and three helices arranged into a partially orthogonal, two-sheet β-barrel, similar to the structure observed in the crystalline Co 2+ complex of full-length DtxR. (pnas.org)
  • Chemical shift perturbation studies demonstrate that a proline-rich peptide corresponding to residues R125-G139 of intact DtxR binds to the C-terminal domain in a pocket formed by residues in β-strands 2, 3, and 5, and helix 3. (pnas.org)
  • From the sequential assignment of resonances in heteronuclear NMR spectra of a recombinant C-terminal domain (residues N130-L226), we have shown that this isolated domain contains five β-strands and three helices ( 14 ). (pnas.org)
  • NMR chemical shift perturbation studies demonstrate that a synthetic peptide corresponding to this internal ligand interacts with specific amino acid residues in the C-terminal domain. (pnas.org)
  • When the Vam7p PX domain was studied in the PtdIns(3) P -bound state and compared with the unligated form, a collection of basic residues that undergo significant chemical shift upon ligation of PtdIns(3) P were identified. (biologists.org)
  • gene
  • PDZ) and extra-cellular signalling ( e.g. integrin-binding RGD), control of gene expression ( e.g. (rsc.org)
  • hERG
  • In contrast, channels that also lacked the CNBHD (hERG Δeag ΔCNBHD-Citrine) were not measurably regulated by N-eag-CFP nor was FRET detected, suggesting that the C-linker/CNBHD was required for eag domains to directly associate with the channel. (rupress.org)
  • Collectively, these findings reveal that the C-linker/CNBHD, but not the S4-S5 linker, was necessary for the eag domain to associate with the channel, that the eag domain and the C-linker/CNBHD were sufficient for a direct interaction, and that an intersubunit interaction between the eag domain and the C-linker/CNBHD regulated slow deactivation in hERG channels at the plasma membrane. (rupress.org)
  • Previous work revealed that the N-terminal eag domain is a key regulator of the characteristic slow deactivation gating in hERG channels. (rupress.org)
  • transmembrane
  • The region between the S4 and S5 transmembrane domains (S4-S5 linker) is also implicated in this process, but the mechanism for regulation of slow deactivation is unclear. (rupress.org)
  • plasma membrane
  • We demonstrated that osmotic stress caused a rapid dissociation of the fluorescence from the plasma membrane of renal epithelial cells expressing GFP-tagged PLCδ1 or its PH domain. (nii.ac.jp)
  • PtdIns
  • In this study we describe two high-resolution crystal structures of the PH domain of PKBalpha in a noncomplexed form and compare this to a new atomic resolution (0.98 A, where 1 A=0.1 nm) structure of the PH domain of PKBalpha complexed to Ins(1,3,4,5)P4, the head group of PtdIns(3,4,5)P3. (rcsb.org)
  • reported a crystal structure of the PX domain of p40 phox bound to dibutanoyl-PtdIns(3) P (a soluble form of PtdIns(3) P ) at 1.7 Å resolution. (biologists.org)
  • Identification
  • Recent work has led to the identification of a p utative p hosphatidylinositol 3,4,5-trisphosphate- b inding m otif (PPBM) at the N-terminal regions of PH domains that interact with this lipid. (biochemj.org)
  • interaction
  • In a FRET hybridization assay, N-eag-CFP had robust FRET with a C-linker/CNBHD-Citrine, suggesting a direct and specific interaction between the eag domain and the C-linker/CNBHD. (rupress.org)
  • The interaction of ERK with CH domains points to a new potential function for CH domains. (biochemj.org)
  • This interaction occurred between the PTB domain of SH2D5 and an NxxF motif located within the N-terminal region of BCR. (mdc-berlin.de)
  • interact
  • Based on these results, we can establish energy thresholds above, or below which, we can predict with 96% confidence that a RA/RB domain will or will not interact with Ras. (crg.eu)
  • Well known examples include SLiMs that interact with 14-3-3, PDZ, SH2, SH3, and WW domains but the true extent and diversity of SLiM-mediated interactions is largely unknown. (rsc.org)
  • conformational
  • Remarkably, in contrast to all other PH domains crystallized so far, our data suggest that binding of Ins(1,3,4,5)P4 to the PH domain of PKB, induces a large conformational change. (rcsb.org)
  • Solution studies with CD also provided evidence of conformational changes taking place upon binding of Ins(1,3,4,5)P4 to the PH domain of PKB. (rcsb.org)
  • mechanism
  • Released GFP-PLCδ1 translocated to perinuclear regions, presumably ER, but the mechanism of targeting may be different from those of PLA2 (and PKC) whose C2 domain may play a role. (nii.ac.jp)
  • localization
  • Thus, the SH3 domain of Myo5p contributes to but is not sufficient for localization of Myo5p either to patches or to sites of polarized cell growth. (rupress.org)