scholarly journals Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: Implications for lipid binding

2000 ◽  
Vol 9 (5) ◽  
pp. 886-897 ◽  
Author(s):  
Brent W. Segelke ◽  
Michael Forstner ◽  
Mark Knapp ◽  
Sergei D. Trakhanov ◽  
Sean Parkin ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Domain Structure ◽  
Conformational Flexibility ◽  
Lipid Binding ◽  
Crystal Forms ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Amino Terminal Domain

Differences in Stability among the Human Apolipoprotein E Isoforms Determined by the Amino-Terminal Domain†

Biochemistry ◽  
2000 ◽  
Vol 39 (38) ◽  
pp. 11657-11666 ◽  
Author(s):  
Julie A. Morrow ◽  
Mark L. Segall ◽  
Sissel Lund-Katz ◽  
Michael C. Phillips ◽  
Mark Knapp ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Human Apolipoprotein ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Amino Terminal Domain

scholarly journals Amino-terminal Domain Stability Mediates Apolipoprotein E Aggregation into Neurotoxic Fibrils

2006 ◽  
Vol 361 (5) ◽  
pp. 932-944 ◽  
Author(s):  
Danny M. Hatters ◽  
Ning Zhong ◽  
Earl Rutenber ◽  
Karl H. Weisgraber
Keyword(s):  
Apolipoprotein E ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Amino Terminal Domain ◽  
Domain Stability

scholarly journals Measles Virus Phosphoprotein Gene Products: Conformational Flexibility of the P/V Protein Amino-Terminal Domain and C Protein Infectivity Factor Function

2004 ◽  
Vol 78 (21) ◽  
pp. 11632-11640 ◽  
Author(s):  
Patricia Devaux ◽  
Roberto Cattaneo
Keyword(s):  
Measles Virus ◽  
Cultured Cells ◽  
Conformational Flexibility ◽  
Particle Assembly ◽  
C Protein ◽  
Amino Terminal ◽  
Terminal Domain ◽  
P Gene ◽  
P Protein ◽  
Amino Terminal Domain

ABSTRACT The measles virus (MV) P gene codes for three proteins: P, an essential polymerase cofactor, and V and C, which have multiple functions but are not strictly required for viral propagation in cultured cells. V shares the amino-terminal domain with P but has a zinc-binding carboxyl-terminal domain, whereas C is translated from an overlapping reading frame. During replication, the P protein binds incoming monomeric nucleocapsid (N) proteins with its amino-terminal domain and positions them for assembly into the nascent ribonucleocapsid. The P protein amino-terminal domain is natively unfolded; to probe its conformational flexibility, we fused it to the green fluorescent protein (GFP), thereby also silencing C protein expression. A recombinant virus (MV-GFP/P) expressing hybrid GFP/P and GFP/V proteins in place of standard P and V proteins and not expressing the C protein was rescued and produced normal ratios of mono-, bi-, and tricistronic RNAs, but its replication was slower than that of the parental virus. Thus, the P protein retained nearly intact polymerase cofactor function, even with a large domain added to its amino terminus. Having noted that titers of cell-associated and especially released MV-GFP/P were reduced and knowing that the C protein of the related Sendai virus has particle assembly and infectivity factor functions, we produced an MV-GFP/P derivative expressing C. Intracellular titers of this virus were almost completely restored, and those of released virus were partially restored. Thus, the MV C protein is an infectivity factor.

Characterization of a Mode of Specific Binding of Fibrin Monomer through its Amino-Terminal Domain by Macrophages and Macrophage Cell-Lines

1990 ◽  
Vol 63 (02) ◽  
pp. 193-203 ◽  
Author(s):  
John R Shainoff ◽  
Deborah J Stearns ◽  
Patricia M DiBello ◽  
Youko Hishikawa-Itoh
Keyword(s):  
Peritoneal Macrophages ◽  
Affinity Binding ◽  
Macrophage Cell ◽  
High Affinity Binding ◽  
Amino Terminal ◽  
High Affinity ◽  
Terminal Domain ◽  
Weak Binding ◽  
Amino Terminal Domain

SummaryThe studies reported here probe the existence of a receptor-mediated mode of fibrin-binding by macrophages that is associated with the chemical change underlying the fibrinogen-fibrin conversion (the release of fibrinopeptides from the amino-terminal domain) without depending on fibrin-aggregation. The question is pursued by 1) characterization of binding in relation to fibrinopeptide content of both the intact protein and the CNBr-fragment comprising the amino-terminal domain known as the NDSK of the protein, 2) tests of competition for binding sites, and 3) photo-affinity labeling of macrophage surface proteins. The binding of intact monomers of types lacking either fibrinopeptide A alone (α-fibrin) or both fibrinopeptides A and B (αβ-fibrin) by peritoneal macrophages is characterized as proceeding through both a fibrin-specific low density/high affinity (BMAX ≃ 200–800 molecules/cell, KD ≃ 10−12 M) interaction that is not duplicated with fibrinogen, and a non-specific high density/low affinity (BMAX ≥ 105 molecules/cell, KD ≥ 10−6 M) interaction equivalent to the weak binding of fibrinogen. Similar binding characteristics are displayed by monocyte/macrophage cell lines (J774A.1 and U937) as well as peritoneal macrophages towards the NDSK preparations of these proteins, except for a slightly weaker (KD ≃ 10−10 M) high-affinity binding. The high affinity binding of intact monomer is inhibitable by fibrin-NDSK, but not fibrinogen-NDSK. This binding appears principally dependent on release of fibrinopeptide-A, because a species of fibrin (β-fibrin) lacking fibrinopeptide-B alone undergoes only weak binding similar to that of fibrinogen. Synthetic Gly-Pro-Arg and Gly-His-Arg-Pro corresponding to the N-termini of to the α- and the β-chains of fibrin both inhibit the high affinity binding of the fibrin-NDSKs, and the cell-adhesion peptide Arg-Gly-Asp does not. Photoaffinity-labeling experiments indicate that polypeptides with elec-trophoretically estimated masses of 124 and 187 kDa are the principal membrane components associated with specifically bound fibrin-NDSK. The binding could not be up-regulated with either phorbol myristyl acetate, interferon gamma or ADP, but was abolished by EDTA and by lipopolysaccharide. Because of the low BMAX, it is suggested that the high-affinity mode of binding characterized here would be too limited to function by itself in scavenging much fibrin, but may act cooperatively with other, less limited modes of fibrin binding.

scholarly journals Role of Amino-Terminal Domain in the Assembly Mechanism of Kainate-Subtype Glutamate Receptor Ion Channels

2014 ◽  
Vol 106 (2) ◽  
pp. 151a
Author(s):  
Sagar Chittori ◽  
Janesh Kumar ◽  
Suvendu Lomash ◽  
Huaying Zhao ◽  
Peter Schuck ◽  
...  
Keyword(s):  
Ion Channels ◽  
Glutamate Receptor ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Assembly Mechanism ◽  
Amino Terminal Domain
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