[49] Membrane proteins: A summary of known structural information

Nelson, David R.; Robinson, N.

doi:10.1016/0076-6879(83)97162-8

Cited by 7 publications

(2 citation statements)

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“…However, not many of the known membrane proteins (see e.g. Nelson & Robinson, 1983) have been isolated in a form pure enough for cyrstallization experiments to seem promising, and a very large number probably remain to be discovered. I hope this review will make the reader familiar with the general approach and some of the specific problems of growing crystals of membrane proteins, and will ultimately stimulate the crystallization of more membrane proteins.…”

Section: Introductionmentioning

confidence: 99%

Three-dimensional crystallization of membrane proteins

Kühlbrandt

1988

Quart. Rev. Biophys.

187

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As recently as 10 years ago, the prospect of solving the structure of any membrane protein by X-ray crystallography seemed remote. Since then, the threedimensional (3-D) structures of two membrane protein complexes, the bacterial photosynthetic reaction centres of Rhodopseudomonas viridis (Deisenhofer et al. 1984, 1985) and of Rhodobacter sphaeroides (Allen et al. 1986, 1987 a, 6; Chang et al. 1986) have been determined at high resolution. This astonishing progress would not have been possible without the pioneering work of Michel and Garavito who first succeeded in growing 3-D crystals of the membrane proteins bacteriorhodopsin (Michel & Oesterhelt, 1980) and matrix porin (Garavito & Rosenbusch, 1980). X-ray crystallography is still the only routine method for determining the 3-D structures of biological macromolecules at high resolution and well-ordered 3-D crystals of sufficient size are the essential prerequisite.

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Section: Introductionmentioning

confidence: 99%

Three-dimensional crystallization of membrane proteins

Kühlbrandt

1988

Quart. Rev. Biophys.

187

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“…In addition, Kalderon et al (1984) have described a short amino acid sequence of SV40 T antigen, Pro-Lys-Lys-Lys-Arg-Lys-Val, which appears to specify the nuclear localization of that protein and which can mediate the transport to the nucleus of chimeric proteins which have been constructed to contain this sequence. This chapter describes experiments which have as their ultimate goal to test the hypothesis that the proteins of the internal membranes of the cell have analogous sequence or structural features which enable the cell to sort them to their correct subcellular compartments (Nelson and Robinson, 1983).…”

Section: A Protein Sorting In Generalmentioning

confidence: 99%