1psy: Difference between revisions

Revision as of 06:24, 28 July 2008

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File:1psy.png

Template:STRUCTURE 1psy

STRUCTURE OF RicC3, NMR, 20 STRUCTURESSTRUCTURE OF RicC3, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 14636051

About this StructureAbout this Structure

1PSY is a Single protein structure of sequence from Ricinus communis. Full experimental information is available from OCA.

ReferenceReference

Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis., Pantoja-Uceda D, Bruix M, Gimenez-Gallego G, Rico M, Santoro J, Biochemistry. 2003 Dec 2;42(47):13839-47. PMID:14636051

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-[[Image:1psy.gif|left|200px]]
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 {{STRUCTURE_1psy|  PDB=1psy  |  SCENE=  }}
-'''STRUCTURE OF RicC3, NMR, 20 STRUCTURES'''
+===STRUCTURE OF RicC3, NMR, 20 STRUCTURES===
-==Overview==
+<!--
-The three-dimensional structure in aqueous solution of recombinant (15)N labeled RicC3, a 2S albumin protein from the seeds of castor bean (Ricinus communis), has been determined by NMR methods. The computed structures were based on 1564 upper limit distance constraints derived from NOE cross-correlation intensities measured in the 2D-NOESY and 3D-HSQC-NOESY experiments, 70 phi torsion angle constraints obtained from (3)J(HNH)(alpha) couplings measured in the HNHA experiment, and 30 psi torsion angle constraints derived from (3)J(H)(alpha)(Ni+1) couplings measured in the HNHB experiment. The computed structures showed a RMSD radius of 0.64 A for the structural core. The resulting structure consists of five amphipatic helices arranged in a right-handed super helix, a folding motif first observed in nonspecific lipid transfer proteins. Different than the latter, RicC3 does have not an internal cavity, a fact that can be related to the exchange in the pairing of disulfide bridges in the segment.CXC. Previous attempts to determine high resolution structures of a 2S albumin protein by either X-ray crystallography or NMR methods failed because of the heterogeneity of the protein prepared from natural sources. Both 2S albumins and nonspecific lipid transfer proteins belong to the prolamine superfamily, some of whose members are food allergens. The solution structure for recombinant RicC3 determined here is a suitable representative structure for the broad family of seed 2S albumin proteins, which may help to establish meaningful relationships between structure and allergenicity. RicC3 is also the peptidic component of the immunomodulator Inmunoferon, a widely used pharmaceutical product, and its structure is expected to help understand its pharmaceutical activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_14636051}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14636051 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14636051}}
 ==About this Structure==
-PSY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PSY OCA].
+PSY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PSY OCA].
 ==Reference==
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 [[Category: Ricc3]]
 [[Category: Seed storage protein]]
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