1qnd

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{{Seed}}
 
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[[Image:1qnd.png|left|200px]]
 
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==STEROL CARRIER PROTEIN-2, NMR, 20 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1qnd", creates the "Structure Box" on the page.
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<StructureSection load='1qnd' size='340' side='right'caption='[[1qnd]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qnd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QND FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qnd OCA], [https://pdbe.org/1qnd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qnd RCSB], [https://www.ebi.ac.uk/pdbsum/1qnd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qnd ProSAT]</span></td></tr>
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{{STRUCTURE_1qnd| PDB=1qnd | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/SCP2_HUMAN SCP2_HUMAN] Leukoencephalopathy-dystonia-motor neuropathy syndrome. The disease is caused by variants affecting the gene represented in this entry. Expression at protein level is almost abolished in Zellweger syndrome. Cholesterol transfer from the endoplasmic reticulum to the plasma membrane was reduced in patient fibroblasts compared to controls.<ref>PMID:7642518</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/SCP2_HUMAN SCP2_HUMAN] Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids (PubMed:10706581). Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA) (PubMed:10706581). Also active with medium and long straight chain 3-oxoacyl-CoAs. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol between membrances, in vitro (By similarity). Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs (By similarity).[UniProtKB:P11915][UniProtKB:P32020]<ref>PMID:10706581</ref> Mediates the transfer of all common phospholipids, cholesterol and gangliosides from the endoplasmic reticulum to the plasma membrane. May play a role in regulating steroidogenesis (PubMed:17157249, PubMed:8300590, PubMed:7642518). Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol (By similarity). Also binds fatty acids and fatty acyl Coenzyme A (CoA) such as phytanoyl-CoA. Involved in the regulation phospholipid synthesis in endoplasmic reticulum enhancing the incorporation of exogenous fatty acid into glycerides. Seems to stimulate the rate-limiting step in phosphatidic acid formation mediated by GPAT3. Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs (By similarity).[UniProtKB:P11915][UniProtKB:P32020]<ref>PMID:17157249</ref> <ref>PMID:7642518</ref> <ref>PMID:8300590</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/1qnd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qnd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone (15)N spin relaxation parameters and NMR studies of nitroxide spin-labeled substrate binding are presented as a new basis for investigations of the mode of action of SCP2. The SCP2 fold is formed by a five-stranded beta-sheet and four alpha-helices. Fatty acid binding to a hydrophobic surface area formed by amino acid residues of the first and third helices, and the beta-sheet, which are all located in the polypeptide segment 8-102, was identified with the use of the spin-labeled substrate 16-doxylstearic acid. In the free protein, the lipid-binding site is covered by the C-terminal segment 105-123, suggesting that this polypeptide segment, which carries the peroxisomal targeting signal (PTS1), might be involved in the regulation of ligand binding.
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===STEROL CARRIER PROTEIN-2, NMR, 20 STRUCTURES===
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NMR structure of the sterol carrier protein-2: implications for the biological role.,Garcia FL, Szyperski T, Dyer JH, Choinowski T, Seedorf U, Hauser H, Wuthrich K J Mol Biol. 2000 Jan 21;295(3):595-603. PMID:10623549<ref>PMID:10623549</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_10623549}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1qnd" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10623549 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10623549}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1QND is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QND OCA].
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==Reference==
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<ref group="xtra">PMID:10623549</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Choinowski, T.]]
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[[Category: Large Structures]]
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[[Category: Dyer, J H.]]
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[[Category: Choinowski T]]
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[[Category: Helmut, H.]]
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[[Category: Dyer JH]]
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[[Category: Lopez-Garcia, F.]]
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[[Category: Hauser H]]
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[[Category: Seedorf, U.]]
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[[Category: Lopez-Garcia F]]
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[[Category: Szyperski, T.]]
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[[Category: Seedorf U]]
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[[Category: Wuthrich, K.]]
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[[Category: Szyperski T]]
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[[Category: Lipid binding]]
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[[Category: Wuthrich K]]
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[[Category: Nitroxide spin label]]
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[[Category: Protein dynamic]]
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[[Category: Protein structure]]
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[[Category: Sterol carrier protein 2]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:55:56 2009''
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Current revision

STEROL CARRIER PROTEIN-2, NMR, 20 STRUCTURES

PDB ID 1qnd

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