Homodimerization and heterodimerization of minimal zinc(II)-binding-domain peptides of T-cell proteins CD4, CD8alpha, and Lck.
Homodimerization and heterodimerization of minimal zinc(II)-binding-domain peptides of T-cell proteins CD4, CD8alpha, and Lck.
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T 细胞蛋白 CD4、CD8α 和 Lck 的最小锌 (II) 结合域肽的同二聚化和异二聚化。
DOI:
10.1021/ja9028928
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发表时间:
2009-08-19
影响因子:
15
通讯作者:
Berg, Jeremy M.
中科院分区:
文献类型:
--
作者:
Davis, Alisa M.;Berg, Jeremy M.
Metal-mediated protein oligomerization is an emerging mode of protein-protein interaction. The C-terminal cytosolic domains of T-cell coreceptors CD4 and CD8α form zinc-bridged heterodimers with the N-terminal region of the kinase Lck, with each protein contributing two cysteinate ligands to the complex. Using size exclusion chromatography, 1H NMR, and UV/visible absorption spectroscopy with cobalt(II) as a spectroscopic probe, we demonstrate that small peptides derived from these regions form metal-bridged heterodimers but also homodimers, in contrast to previous reports. The Lck-CD4 and Lck-CD8α cobalt(II)-bridged heterodimer complexes are more stable than the corresponding (Lck)2cobalt(II) complex by factors of 11 ± 4 and 22 ± 9, respectively. These studies were aided by the discovery that cobalt(II) complexes with a cobalt(II)(-Cys-X-X-Cys-)(-Cys-X-Cys-) chromophore show unusual optical spectra with one component of the visible d to d (4A2 to 4T1(P)) transition red-shifted and well separated from the other components. These results provide insights into the basis of specificity of metal-bridged complex formation and on the potential biological significance of metal-bridged homodimers in T-cells.
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影响因子:
3.5
作者:
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通讯作者:
GACON, G
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DOI:
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发表时间:
1997-06-01
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通讯作者:
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DOI:
10.1098/rstb.1988.0058
发表时间:
1988-07-06
影响因子:
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作者:
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通讯作者:
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