期刊
BIOCHEMISTRY
卷 40, 期 9, 页码 2808-2815出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi0027276
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资金
- NCRR NIH HHS [RR00995] Funding Source: Medline
- NHLBI NIH HHS [HL61001] Funding Source: Medline
The ligand-binding domain of the LDL receptor consists of seven contiguous LDL-A modules. The fifth of these ligand-binding modules is absolutely required for recognition of both LDL and beta -VLDL particles. A four-residue linker of variable sequence connects each pair of modules, except for modules four and five, which are connected by a 12-residue linker. To provide a more detailed understanding of the structural relationship in a typical pair of functionally important LDL-A repeats of the LDLR, we investigated the backbone dynamics of repeats five (LR5) and six (LR6) alone and in the context of the covalently connected LR5-6 pair. Our results reveal substantial flexibility in the four-residue linker connecting the two repeats in the LR5-6 pair. The intrinsic dynamic behavior of each repeat is essentially unchanged when the repeats are covalently connected. These observations indicate that the relative orientation of repeats in LR5-6 is not fixed. Modeled in an extended conformation, the linker can separate LR5 and LR6 by up to 15 Angstrom, a distance that would allow substantial freedom of motion of each repeat with respect to the other in the pair.
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