1hll: Difference between revisions

Revision as of 08:21, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1hll.png

Template:STRUCTURE 1hll

NMR STRUCTURE OF T3-I2, A 32 RESIDUE PEPTIDE FROM THE ALPHA-2A ADRENERGIC RECEPTORNMR STRUCTURE OF T3-I2, A 32 RESIDUE PEPTIDE FROM THE ALPHA-2A ADRENERGIC RECEPTOR

Template:ABSTRACT PUBMED 11888275

About this StructureAbout this Structure

1HLL is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

NMR structure of the second intracellular loop of the alpha 2A adrenergic receptor: evidence for a novel cytoplasmic helix., Chung DA, Zuiderweg ER, Fowler CB, Soyer OS, Mosberg HI, Neubig RR, Biochemistry. 2002 Mar 19;41(11):3596-604. PMID:11888275

Page seeded by OCA on Tue Jul 1 08:21:49 2008

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OCA

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-[[Image:1hll.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1hll|  PDB=1hll  |  SCENE=  }}
-'''NMR STRUCTURE OF T3-I2, A 32 RESIDUE PEPTIDE FROM THE ALPHA-2A ADRENERGIC RECEPTOR'''
+===NMR STRUCTURE OF T3-I2, A 32 RESIDUE PEPTIDE FROM THE ALPHA-2A ADRENERGIC RECEPTOR===
-==Overview==
+<!--
-A major, unresolved question in signal transduction by G protein coupled receptors (GPCRs) is to understand how, at atomic resolution, a GPCR activates a G protein. A step toward answering this question was made with the determination of the high-resolution structure of rhodopsin; we now know the intramolecular interactions that characterize the resting conformation of a GPCR. To what degree does this structure represent a structural paradigm for other GPCRs, especially at the cytoplasmic surface where GPCR-G protein interaction occurs and where the sequence homology is low among GPCRs? To address this question, we performed NMR studies on approximately 35-residue-long peptides including the critical second intracellular loop (i2) of the alpha 2A adrenergic receptor (AR) and of rhodopsin. To stabilize the secondary structure of the peptide termini, 4-12 residues from the adjacent transmembrane helices were included and structures determined in dodecylphosphocholine micelles. We also characterized the effects on an alpha 2A AR peptide of a D130I mutation in the conserved DRY motif. Our results show that in contrast to the L-shaped loop in the i2 of rhodopsin, the i2 of the alpha 2A AR is predominantly helical, supporting the hypothesis that there is structural diversity within GPCR intracellular loops. The D130I mutation subtly modulates the helical structure. The spacing of nonpolar residues in i2 with helical periodicity is a predictor of helical versus loop structure. These data should lead to more accurate models of the intracellular surface of GPCRs and of receptor-mediated G protein activation.
+The line below this paragraph, {{ABSTRACT_PUBMED_11888275}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11888275 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11888275}}
 ==About this Structure==
-HLL is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLL OCA].
+HLL is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLL OCA].
 ==Reference==
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 [[Category: Zuiderweg, E R.P.]]
 [[Category: Helix-linker-helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:59:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:21:49 2008''