The Basic Protein of CNS Myelin: Its Structure and Ligand Binding
The Basic Protein of CNS Myelin: Its Structure and Ligand Binding
复制标题
中枢神经系统髓磷脂的基础蛋白:其结构和配体结合
DOI:
--
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发表时间:
1992
影响因子:
4.7
通讯作者:
Ross C. Smith
中科院分区:
文献类型:
--
作者:
Ross C. Smith
Consideration of the evidence presented in this review leads to the following conclusions: (a) Isolated MBP in aqueous solution has little ordered secondary or tertiary structure. (b) In this state, the protein can associate with a wide range of hydrophobic and amphiphilic compounds, these interactions involving limited sections of the protein. (c) The strength of binding to bilayers and the accompanying conformational changes in the protein are greatest for systems containing acidic lipids, presumably because of the involvement of ionic interactions. (d) When bound to bilayers of acidic lipids, MBP will have substantially more ordered secondary structure than it manifests in aqueous solution, and it is likely to be oligomeric (possibly hexameric). (e) MBP does affect the organization of lipid aggregates. It influences strongly the separation of bilayers in multilayers of purified lipids, and at present this must be viewed as its prime role within myelin. The greatest impediment to our understanding of MBP is the lack of an assayable biological activity. In contrast to the situation with enzymes, for example, we have no functional test for changes in protein structure or changes accompanying interactions with other molecules. Current evidence suggests that the protein has a structural role within myelin and that its own three-dimensional structure is strongly dependent on the molecules with which it is associated. If this picture is correct, studies of the isolated protein or of the protein in reconstituted lipid systems may yield, at best, a rough guide to the structure within its biological environment. Further clarification of the structure and function of MBP may have to await development of more powerful techniques for studying proteins bound to large molecular aggregates, such as lipid bilayers. The paucity of generally applicable methods is reflected in the fact that even low resolution structures are known for only a handful of intrinsic membrane proteins, and even more limited information exists for proteins associated with membrane surfaces. However, the increasing use of a combination of electron microscopy and diffraction on two-dimensional arrays of proteins formed on lipid bilayers (Henderson et al., 1990) offers the hope that it may not be too long before it will be possible to study at moderate resolution the three-dimensional structure of MBP bound to a lipid membrane.
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DOI:
--
发表时间:
1987
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Maggio,B;Sturtevant,JM;Yu,RK
通讯作者:
Yu,RK
DOI:
10.1042/bj2440001
发表时间:
1987-05
期刊:
The Biochemical journal
影响因子:
--
作者:
Martin G. Low
通讯作者:
Martin G. Low
DOI:
10.1042/bj2480285
发表时间:
1987
期刊:
The Biochemical journal
影响因子:
--
作者:
Smith,R;Braun,PE;Ferguson,MA;Low,MG;Sherman,WR
通讯作者:
Sherman,WR
DOI:
10.1016/0005-2736(82)90105-5
发表时间:
1982
期刊:
Biochimica et biophysica acta
影响因子:
--
作者:
Epand,RM;Moscarello,MA
通讯作者:
Moscarello,MA
影响因子:
5.6
作者:
HENDERSON, R;BALDWIN, JM;DOWNING, KH
通讯作者:
DOWNING, KH