1fdf: Difference between revisions
New page: left|200px<br /><applet load="1fdf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fdf" /> '''HELIX 7 BOVINE RHODOPSIN'''<br /> ==Overvie... |
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'''HELIX 7 BOVINE RHODOPSIN'''<br /> | '''HELIX 7 BOVINE RHODOPSIN'''<br /> | ||
==Overview== | ==Overview== | ||
PURPOSE: The three dimensional structure of a peptide comprising the | PURPOSE: The three dimensional structure of a peptide comprising the sequence of the seventh transmembrane segment of the G-protein coupled receptor, rhodopsin, was determined in solution. METHODS: The sequence of the seventh transmembrane segment of rhodopsin, which contains the NPxxY sequence that is highly conserved among G-protein coupled receptors and lys296 that forms the Schiff base with the retinal, was synthesized by solid phase peptide synthesis. The three dimensional structure was determined in solution by high-resolution nuclear magnetic resonance (NMR). RESULTS: The structure revealed a helix-break-helix motif for this sequence. Two families of structures were observed which differed in the angle between the two helical segments. The sequence of this transmembrane segment overlapped significantly the sequence of a peptide from the carboxyl terminal of rhodopsin, the structure of which was solved previously. The redundant sequence formed a helix in both peptides. It was therefore possible to superimpose the redundant sequence of both peptides and construct a structure for rhodopsin encompassing residues 291-348. CONCLUSIONS: This structure reveals locations of the lys296 and the acylation sites of rhodopsin that are consistent with the known biochemistry of this receptor. This segmentation approach to membrane protein structure provides important structural information in the absence of an X-ray crystal structure of rhodopsin. The approach is expected to be useful for other G-protein coupled receptors. | ||
==About this Structure== | ==About this Structure== | ||
1FDF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | 1FDF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDF OCA]. | ||
==Reference== | ==Reference== | ||
Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin., Yeagle PL, Danis C, Choi G, Alderfer JL, Albert AD, Mol Vis. 2000 Jul 27;6:125-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10930473 10930473] | Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin., Yeagle PL, Danis C, Choi G, Alderfer JL, Albert AD, Mol Vis. 2000 Jul 27;6:125-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10930473 10930473] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Albert, A | [[Category: Albert, A D.]] | ||
[[Category: Alderfer, J | [[Category: Alderfer, J L.]] | ||
[[Category: Choi, G.]] | [[Category: Choi, G.]] | ||
[[Category: Danis, C.]] | [[Category: Danis, C.]] | ||
[[Category: Yeagle, P | [[Category: Yeagle, P L.]] | ||
[[Category: helix]] | [[Category: helix]] | ||
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Revision as of 13:37, 21 February 2008
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HELIX 7 BOVINE RHODOPSIN
OverviewOverview
PURPOSE: The three dimensional structure of a peptide comprising the sequence of the seventh transmembrane segment of the G-protein coupled receptor, rhodopsin, was determined in solution. METHODS: The sequence of the seventh transmembrane segment of rhodopsin, which contains the NPxxY sequence that is highly conserved among G-protein coupled receptors and lys296 that forms the Schiff base with the retinal, was synthesized by solid phase peptide synthesis. The three dimensional structure was determined in solution by high-resolution nuclear magnetic resonance (NMR). RESULTS: The structure revealed a helix-break-helix motif for this sequence. Two families of structures were observed which differed in the angle between the two helical segments. The sequence of this transmembrane segment overlapped significantly the sequence of a peptide from the carboxyl terminal of rhodopsin, the structure of which was solved previously. The redundant sequence formed a helix in both peptides. It was therefore possible to superimpose the redundant sequence of both peptides and construct a structure for rhodopsin encompassing residues 291-348. CONCLUSIONS: This structure reveals locations of the lys296 and the acylation sites of rhodopsin that are consistent with the known biochemistry of this receptor. This segmentation approach to membrane protein structure provides important structural information in the absence of an X-ray crystal structure of rhodopsin. The approach is expected to be useful for other G-protein coupled receptors.
About this StructureAbout this Structure
1FDF is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin., Yeagle PL, Danis C, Choi G, Alderfer JL, Albert AD, Mol Vis. 2000 Jul 27;6:125-31. PMID:10930473
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