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1lvz

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[[Image:1lvz.gif|left|200px]]
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{{STRUCTURE_1lvz| PDB=1lvz | SCENE= }}
{{STRUCTURE_1lvz| PDB=1lvz | SCENE= }}
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'''METARHODOPSIN II BOUND STRUCTURE OF C-TERMINAL PEPTIDE OF ALPHA-SUBUNIT OF TRANSDUCIN'''
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===METARHODOPSIN II BOUND STRUCTURE OF C-TERMINAL PEPTIDE OF ALPHA-SUBUNIT OF TRANSDUCIN===
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==Overview==
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Residual dipolar couplings for a ligand that is in fast exchange between a free state and a state where it is bound to a macroscopically ordered membrane protein carry precise information on the structure and orientation of the bound ligand. The couplings originate in the bound state but can be detected on the free ligand using standard high resolution NMR. This approach is used to study an analog of the C-terminal undecapeptide of the alpha-subunit of the heterotrimeric G protein transducin when bound to photo-activated rhodopsin. Rhodopsin is the major constituent of disk-shaped membrane vesicles from rod outer segments of bovine retinas, which align spontaneously in the NMR magnet. Photo-activation of rhodopsin triggers transient binding of the peptide, resulting in measurable dipolar contributions to 1J(NH) and 1J(CH) splittings. These dipolar couplings report on the time-averaged orientation of bond vectors in the bound peptide relative to the magnetic field, i.e. relative to the membrane normal. Approximate distance restraints of the bound conformation were derived from transferred NOEs, as measured from the difference of NOESY spectra recorded prior to and after photo-activation. The N-terminal eight residues of the bound undecapeptide adopt a near-ideal alpha-helical conformation. The helix is terminated by an alpha(L) type C-cap, with Gly9 at the C' position in the center of the reverse turn. The angle between the helix axis and the membrane normal is 40 degrees (+/-4) degrees. Peptide protons that make close contact with the receptor are identified by analysis of the NOESY cross-relaxation pattern and include the hydrophobic C terminus of the peptide.
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(as it appears on PubMed at http://www.pubmed.gov), where 12217702 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12217702}}
==About this Structure==
==About this Structure==
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1LVZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LVZ OCA].
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1LVZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LVZ OCA].
==Reference==
==Reference==
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[[Category: Alpha helix]]
[[Category: Alpha helix]]
[[Category: Rhodopsin-transducin complex]]
[[Category: Rhodopsin-transducin complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:21:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:33:54 2008''

Revision as of 19:34, 2 July 2008

Image:1lvz.png

Template:STRUCTURE 1lvz

METARHODOPSIN II BOUND STRUCTURE OF C-TERMINAL PEPTIDE OF ALPHA-SUBUNIT OF TRANSDUCIN

Template:ABSTRACT PUBMED 12217702

About this Structure

1LVZ is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.

Reference

Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings., Koenig BW, Kontaxis G, Mitchell DC, Louis JM, Litman BJ, Bax A, J Mol Biol. 2002 Sep 13;322(2):441-61. PMID:12217702

Page seeded by OCA on Wed Jul 2 22:33:54 2008

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