Zobrazeno 1 - 9
of 9
pro vyhledávání: '"D. F. Wyss"'
Autor:
S. J. Davis, P. A. van der Merwe, E. L. Reinherz, J. Li, A. Smoylar, D. F. Wyss, M. H. Knoppers, K. J. Willis, A. R. N. Arulanandam, J. S. Choi, G. Wagner
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daa65daa48faabebe5cbb6f9445e27ce
https://ora.ox.ac.uk/objects/uuid:b858ddec-1cf8-441e-87e4-43d824ee7650
https://ora.ox.ac.uk/objects/uuid:b858ddec-1cf8-441e-87e4-43d824ee7650
Publikováno v:
Journal of molecular biology. 314(3)
The NS3 protein of the hepatitis C virus (HCV) is a 631 amino acid residue bifunctional enzyme with a serine protease localized to the N-terminal 181 residues and an RNA helicase located in the C-terminal 450 residues. The HCV NS3 RNA helicase consis
Publikováno v:
Journal of biomolecular NMR. 19(3)
Autor:
M A, McCoy, D F, Wyss
Publikováno v:
Journal of biomolecular NMR. 18(3)
Structural studies of protein-ligand complexes are often limited by low solubility, poor affinity, and interfacial motion and, in NMR structures, by the lack of intermolecular NOEs. In the absence of other structural restraints, we use a procedure th
Publikováno v:
Journal of biomolecular NMR. 18(3)
Publikováno v:
Nature structural biology. 6(6)
Using NMR spectroscopy, we determined the solution structure of a single-chain T-cell receptor (scTCR) derived from the major histocompatibility complex (MHC) class II-restricted D10 TCR. The conformations of complementarity-determining regions (CDRs
Publikováno v:
Protein science : a publication of the Protein Society. 6(3)
We have used 15N NMR relaxation experiments to probe, for the glycosylated human CD2 adhesion domain, the overall molecular motion, as well as very fast nanosecond-picosecond (ns-ps) and slow millisecond-microsecond (ms-microsecond) internal motions.
Publikováno v:
Biochemistry. 34(5)
CD2, a T cell specific surface adhesion receptor, is critically important for T lymphocytes to mediate their regulatory and effector functions. The amino terminal domain of human CD2 is responsible for cell adhesion, binding to CD58 on antigen-presen
Publikováno v:
Biochemistry. 32(41)
Human CD2, a glycosylated transmembrane receptor found on all T-lymphocytes, plays a key role in facilitating cellular adhesion between T-cells and target cells or antigen-presenting cells by binding to its counter receptor CD58 (LFA-3) present on th