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Chou, James J.; Gaemers, Sander; Howder, Bernard; Louis, John M.; Bax, Ad

doi:10.1023/a:1013336502594

Cited by 235 publications

(123 citation statements)

References 13 publications

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“…Polymerization was initiated by the addition of ammonium persulfate and TEMED at 0.1% w/v and v/v, respectively, and allowed to proceed in a cylinder of 5.4-mm diameter for 3 h at 23°C. Subsequently, gels were dialyzed, dried, soaked with protein solution for 2 days, and transferred to NMR tubes as described (24,25).…”

Section: Methodsmentioning

confidence: 99%

Structure and Dynamics of Micelle-bound Human α-Synuclein

Ulmer¹,

Bax²,

Cole

et al. 2005

Journal of Biological Chemistry

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860

1,168

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Misfolding of the protein ␣-synuclein (aS), which associates with presynaptic vesicles, has been implicated in the molecular chain of events leading to Parkinson's disease. Here, the structure and dynamics of micelle-bound aS are reported. A dynamic variation in interhelical distance on the microsecond timescale is complemented by enhanced sub-nanosecond timescale dynamics, particularly in the remarkably glycine-rich segments of the helices. These unusually rich dynamics may serve to mitigate the effect of aS binding on membrane fluidity. The well ordered conformation of the helix-helix connector indicates a defined interaction with lipidic surfaces, suggesting that, when bound to larger diameter synaptic vesicles, it can act as a switch between this structure and a previously proposed uninterrupted helix.

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Section: Methodsmentioning

confidence: 99%

Structure and Dynamics of Micelle-bound Human α-Synuclein

Ulmer¹,

Bax²,

Cole

et al. 2005

Journal of Biological Chemistry

Self Cite

860

1,168

View full text Add to dashboard Cite

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“…Aromatic side chain chemical shifts were assigned with 2D DQF-COSY and 2D NOESY ( m ϭ 120 ms) experiments by using 15 N-labeled protein samples in 99.9% D 2 O. Stereospecific chemical shift assignments for valine and leucine methyl groups were obtained with two constant-time 1 H/ 13 C-HSQC experiments (28-and 43-ms delay) by using 10% 13 C-labeled samples (28). Residual dipolar couplings were extracted from in-phase antiphase experiments by using 15 N-labeled samples aligned in 5% polyacrylamide stretched gels (29). Distance restraints were obtained from 3D 15 N-edited NOESY ( m ϭ 150 ms) and 13 C-edited NOESY ( m ϭ 100 ms) spectra recorded from 15 N-or 15 N, 13 C-labeled proteins.…”

Section: Methodsmentioning

confidence: 99%

Signal transduction pathway of TonB-dependent transporters

Ferguson

Amezcua²,

Halabi³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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Transcription of the ferric citrate import system is regulated by ferric citrate binding to the outer membrane transporter FecA. A signal indicating transporter occupancy is relayed across the outer membrane to energy-transducing and regulatory proteins embedded in the cytoplasmic membrane. Because transcriptional activation is not coupled to ferric citrate import, an allosteric mechanism underlies this complex signaling mechanism. Using evolutionbased statistical analysis we have identified a sparse but structurally connected network of residues that links distant functional sites in FecA. Functional analyses of these positions confirm their involvement in the mechanism that regulates transcriptional activation in response to ferric citrate binding at the cell surface. This mechanism appears to be conserved and provides the structural basis for the allosteric signaling of TonB-dependent transporters.bacterial iron transport ͉ NMR ͉ signaling domain ͉ statistical coupling analysis

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“…Polyacrylamide gel (4.8%) was used to align the sample. The samples were prepared by using the apparatus developed by Chou et al (38) and purchased from New Era Enterprise (Vineland, NJ), following a similar protocol to that described by Mohana-Borges et al (39). The RDCs of resolved 1 H-15 N were measured by using the IPAP scheme (40) for both components of the complex (41).…”

Section: Methodsmentioning

confidence: 99%

Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1β

Zhang

DeRider

McCornack

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

104

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Chemokines (chemotactic cytokines) comprise a large family of proteins that recruit and activate leukocytes, giving chemokines a major role in both immune response and inflammation-related diseases. The poxvirus-encoded viral CC chemokine inhibitor (vCCI) binds to many CC chemokines with high affinity, acting as a potent inhibitor of chemokine action. We have used heteronuclear multidimensional NMR to determine the structure of an orthopoxvirus vCCI in complex with a human CC chemokine, MIP-1␤ (macrophage inflammatory protein 1␤). vCCI binds to the chemokine with 1:1 stoichiometry, forming a complex of 311 aa. vCCI uses residues from its ␤-sheet II to interact with a surface of MIP-1␤ that includes residues adjacent to its N terminus, as well as residues in the 20 s region and the 40 s loop. This structure reveals the strategy used by vCCI to tightly bind numerous chemokines while retaining selectivity for the CC chemokine subfamily.inflammation ͉ protein:protein complex ͉ NMR ͉ chemokine-binding protein

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Untitled

Cited by 235 publications

References 13 publications

Structure and Dynamics of Micelle-bound Human α-Synuclein

Structure and Dynamics of Micelle-bound Human α-Synuclein

Signal transduction pathway of TonB-dependent transporters

Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1β

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