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Results 1 - 10
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72
MagicWand: A Single, Designed Peptide That Assembles to Stable, Ordered
, 2008
"... ABSTRACT: We describe a straightforward single-peptide design that self-assembles into extended and thickened nano-to-mesoscale fibers of remarkable stability and order. The basic chassis of the design is the well-understood dimeric R-helical coiled-coil motif. As such, the peptide has a heptad sequ ..."
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ABSTRACT: We describe a straightforward single-peptide design that self-assembles into extended and thickened nano-to-mesoscale fibers of remarkable stability and order. The basic chassis of the design is the well-understood dimeric R-helical coiled-coil motif. As such, the peptide has a heptad
Side-chain pairing preferences in the parallel coiled-coil dimer motif: Insight on ion pairing between core and flanking sites
- J Am Chem Soc
, 2010
"... Proteins collectively display a broad array of tertiary and quaternary structures, with many different modes of packing between neighboring secondary structure elements. Among the possibilities, the R-helical coiled coil is unusual in that it is both common and regular.1 In the simplest case, two R- ..."
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Cited by 2 (1 self)
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Proteins collectively display a broad array of tertiary and quaternary structures, with many different modes of packing between neighboring secondary structure elements. Among the possibilities, the R-helical coiled coil is unusual in that it is both common and regular.1 In the simplest case, two R-helices
Structural Basis for the Oligomerization-State Switch from a Dimer to a Trimer of an Engineered Cortexillin-1 Coiled-Coil Variant
"... Coiled coils are well suited to drive subunit oligomerization and are widely used in applications ranging from basic research to medicine. The optimization of these applications requires a detailed understanding of the molecular determinants that control of coiled-coil formation. Although many of th ..."
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the unrelated coiled-coil domains from GCN4, ATF1 and cortexillin-1 as model systems. We found that well-known trimer-specific oligomerization-state determinants, such as the distribution of isoleucine residues at heptad-repeat core positions or the trimerization motif Arg-h-x-x-h-Glu (where h = hydrophobic
Dimerization of CtIP, a BRCA1- and CtBP-interacting Protein, Is Mediated by an N-terminal Coiled-coil Motif*
"... CtIP is a transcriptional co-regulator that binds a num-ber of proteins involved in cell cycle control and cell de-velopment, such as CtBP (C terminus-binding protein), BRCA1 (breast cancer-associated protein-1), and LMO4 (LIM-only protein-4). The only recognizable structural motifs within CtIP are ..."
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IP are two putative coiled-coil domains located near the N and C termini of the protein. We now show that the N-terminal coiled coil (residues 45–160), but not the C-terminal coiled coil, mediates homodimeriza-tion of CtIP in mammalian 293T cells. The N-terminal coiled coil did not facilitate binding to LMO4
Crystal Structure of a Coiled-Coil Domain from Human
, 2010
"... The small GTPase Rho and one of its targets, Rho-associated kinase (ROCK), participate in a variety of actin-based cellular processes including smooth muscle contraction, cell migration, and stress fiber formation. The ROCK protein consists of an N-terminal kinase domain, a central coiled-coil domai ..."
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Cited by 4 (0 self)
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domain containing a Rho binding site, and a C-terminal pleckstrin homology domain. Here we present the crystal structure of a large section of the central coiled-coil domain of human ROCK I (amino acids 535–700). The structure forms a parallel a-helical coiled-coil dimer that is structurally similar
Structural Basis of ZIP Occurrence of ZIP and Coiled-coil Motifs Dimerization Specificity of ZIP
"... The leucine zipper (ZIP) motif consists of a periodic repetition of a leucine residue at every seventh position and forms an a-helical conformation, which facilitates dimerization and in some cases higher oligomerization of proteins. In many eukaryotic gene regulatory proteins, the ZIP motif is flan ..."
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The leucine zipper (ZIP) motif consists of a periodic repetition of a leucine residue at every seventh position and forms an a-helical conformation, which facilitates dimerization and in some cases higher oligomerization of proteins. In many eukaryotic gene regulatory proteins, the ZIP motif
Molecular-Scale Force Measurement in a Coiled-Coil Peptide Dimer by Electron Spin Resonance
, 2009
"... Fabrication of multicomponent nanostructures requires the as-sembly of molecular-scale components into ordered arrays. Biology offers examples of self-assembling structures that form functional entities.1 Coiled-coil peptides are a particularly interesting class of biological models that naturally f ..."
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Cited by 1 (1 self)
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at the nanoscale level.4,5 In this communication we demonstrate a new experimental method for measuring intercoil forces that is based on electron spin labeling and double electron-electron resonance (DEER) spec-troscopy. The model system used for these measurements is derived from the R-helical coiled-coil
Investigating the tolerance of coiled-coil peptides to nonheptad sequence inserts
- J. Struct. Biol
, 2002
"... Coiled-coil motifs foster a wide variety of proteinprotein interactions. Canonical coiled coils are based on 7-residue repeats, which guide the folding and assembly of amphipathic ␣-helices. In many cases such repeats remain unbroken for tens to hundreds of residues. However, the sequences of an in ..."
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Cited by 5 (3 self)
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Coiled-coil motifs foster a wide variety of proteinprotein interactions. Canonical coiled coils are based on 7-residue repeats, which guide the folding and assembly of amphipathic ␣-helices. In many cases such repeats remain unbroken for tens to hundreds of residues. However, the sequences
Mcm10 Self-Association Is Mediated by an N-Terminal Coiled-Coil Domain
, 2013
"... Minichromosome maintenance protein 10 (Mcm10) is an essential eukaryotic DNA-binding replication factor thought to serve as a scaffold to coordinate enzymatic activities within the replisome. Mcm10 appears to function as an oligomer rather than in its monomeric form (or rather than as a monomer). Ho ..."
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Cited by 1 (1 self)
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). However, various orthologs have been found to contain 1, 2, 3, 4, or 6 subunits and thus, this issue has remained controversial. Here, we show that self-association of Xenopus laevis Mcm10 is mediated by a conserved coiled-coil (CC) motif within the N-terminal domain (NTD). Crystallographic analysis
Cingulin contains globular and coiled-coil domains and interacts with ZO-1, ZO-2, ZO-3, and myosin
- J. Cell
, 1999
"... Abstract. We characterized the sequence and protein interactions of cingulin, an M r 140–160-kD phosphoprotein localized on the cytoplasmic surface of epithelial tight junctions (TJ). The derived amino acid sequence of a full-length Xenopus laevis cingulin cDNA shows globular head (residues 1–439) a ..."
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Cited by 33 (1 self)
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–439) and tail (1,326– 1,368) domains and a central �-helical rod domain (440–1,325). Sequence analysis, electron microscopy, and pull-down assays indicate that the cingulin rod is responsible for the formation of coiled-coil parallel dimers, which can further aggregate through intermolecular interactions. Pull
Results 1 - 10
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72
