New NMR assignment 1H, 13C, and 15N assignment of the second PH domain of human pleckstrin (234-350)
New NMR assignment 1H, 13C, and 15N assignment of the second PH domain of human pleckstrin (234-350)
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DOI：
10.1007/s10858-005-6053-x
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发表时间：
2006-01-01
影响因子：
2.7
通讯作者：
Muhle-Goll, Claudia
中科院分区：
文献类型：
--
作者：
Edlich, Christian;Simon, Bernd;Muhle-Goll, Claudia
Pleckstrin is the major target of protein kinase C (PKC) in blood platelets (Lyons and Atherton, 1979). It consists of 3 domains: a pleckstrin homology (PH) domain at each terminus and a central DEP domain. The structures of both the N-terminal PH domain and the DEP domain have been previously determined by NMR. In order to assemble full-length pleckstrin from its constituting domains we solved the structure of the third domain of pleckstrin, C–PH by NMR. 2D and 3D heteronuclear NMR experiments were performed with 13C, 15N-labeled C–PH (residues 234–350). Most of the resonances were assigned with the exception of the carbonyl atoms, the N resonances of the prolines and the N-terminal His6-tag. The resonances of the b1–b2 loop (H236, R237, R238, K239) were also not assigned, most likely because of conformational exchange on intermediate time-scales. The assignments have been deposited in the BioMagResBank under accession number 6873.
