1qnd: Difference between revisions

Revision as of 17:16, 29 September 2014

STEROL CARRIER PROTEIN-2, NMR, 20 STRUCTURES

Structural highlights

1qnd is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Disease

[NLTP_HUMAN] Defects in SCP2 are a cause of leukoencephalopathy with dystonia and motor neuropathy (LDMN) [MIM:613724]; also known as sterol carrier protein 2 deficiency. LDMN is a syndrome characterized by leukoencephalopathy, dystonic head tremor, spasmodic torticollis and reduced tendon reflexes in lower extremities. Additional features include hyposmia, pathologic saccadic eye movements, a slight hypoacusis, accumulation of branched-chain pristanic acid in plasma, and the presence of abnormal bile alcohol glucuronides in urine.^[1]

Function

[NLTP_HUMAN] Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis.^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ferdinandusse S, Kostopoulos P, Denis S, Rusch H, Overmars H, Dillmann U, Reith W, Haas D, Wanders RJ, Duran M, Marziniak M. Mutations in the gene encoding peroxisomal sterol carrier protein X (SCPx) cause leukencephalopathy with dystonia and motor neuropathy. Am J Hum Genet. 2006 Jun;78(6):1046-52. Epub 2006 Mar 29. PMID:16685654 doi:10.1086/503921
↑ Seedorf U, Scheek S, Engel T, Steif C, Hinz HJ, Assmann G. Structure-activity studies of human sterol carrier protein 2. J Biol Chem. 1994 Jan 28;269(4):2613-8. PMID:8300590
↑ Stanley WA, Filipp FV, Kursula P, Schuller N, Erdmann R, Schliebs W, Sattler M, Wilmanns M. Recognition of a functional peroxisome type 1 target by the dynamic import receptor pex5p. Mol Cell. 2006 Dec 8;24(5):653-63. PMID:17157249 doi:10.1016/j.molcel.2006.10.024
↑ Garcia FL, Szyperski T, Dyer JH, Choinowski T, Seedorf U, Hauser H, Wuthrich K. NMR structure of the sterol carrier protein-2: implications for the biological role. J Mol Biol. 2000 Jan 21;295(3):595-603. PMID:10623549 doi:10.1006/jmbi.1999.3355

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Ferdinandusse S, Kostopoulos P, Denis S, Rusch H, Overmars H, Dillmann U, Reith W, Haas D, Wanders RJ, Duran M, Marziniak M. Mutations in the gene encoding peroxisomal sterol carrier protein X (SCPx) cause leukencephalopathy with dystonia and motor neuropathy. Am J Hum Genet. 2006 Jun;78(6):1046-52. Epub 2006 Mar 29. PMID:16685654 doi:10.1086/503921

[2] Seedorf U, Scheek S, Engel T, Steif C, Hinz HJ, Assmann G. Structure-activity studies of human sterol carrier protein 2. J Biol Chem. 1994 Jan 28;269(4):2613-8. PMID:8300590

[3] Stanley WA, Filipp FV, Kursula P, Schuller N, Erdmann R, Schliebs W, Sattler M, Wilmanns M. Recognition of a functional peroxisome type 1 target by the dynamic import receptor pex5p. Mol Cell. 2006 Dec 8;24(5):653-63. PMID:17157249 doi:10.1016/j.molcel.2006.10.024

[4] Garcia FL, Szyperski T, Dyer JH, Choinowski T, Seedorf U, Hauser H, Wuthrich K. NMR structure of the sterol carrier protein-2: implications for the biological role. J Mol Biol. 2000 Jan 21;295(3):595-603. PMID:10623549 doi:10.1006/jmbi.1999.3355

[1]

[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-{{STRUCTURE_1qnd|  PDB=1qnd  |  SCENE=  }}
+==STEROL CARRIER PROTEIN-2, NMR, 20 STRUCTURES==
-===STEROL CARRIER PROTEIN-2, NMR, 20 STRUCTURES===
+<StructureSection load='1qnd' size='340' side='right' caption='[[1qnd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
-{{ABSTRACT_PUBMED_10623549}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1qnd]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QND FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qnd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qnd RCSB], [http://www.ebi.ac.uk/pdbsum/1qnd PDBsum]</span></td></tr>
+<table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/NLTP_HUMAN NLTP_HUMAN]] Defects in SCP2 are a cause of leukoencephalopathy with dystonia and motor neuropathy (LDMN) [MIM:[http://omim.org/entry/613724 613724]]; also known as sterol carrier protein 2 deficiency. LDMN is a syndrome characterized by leukoencephalopathy, dystonic head tremor, spasmodic torticollis and reduced tendon reflexes in lower extremities. Additional features include hyposmia, pathologic saccadic eye movements, a slight hypoacusis, accumulation of branched-chain pristanic acid in plasma, and the presence of abnormal bile alcohol glucuronides in urine.<ref>PMID:16685654</ref>
+== Function ==
+[[http://www.uniprot.org/uniprot/NLTP_HUMAN NLTP_HUMAN]] Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis.<ref>PMID:8300590</ref> <ref>PMID:17157249</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/1qnd_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==Disease==
+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>
-[[http://www.uniprot.org/uniprot/NLTP_HUMAN NLTP_HUMAN]] Defects in SCP2 are a cause of leukoencephalopathy with dystonia and motor neuropathy (LDMN) [MIM:[http://omim.org/entry/613724 613724]]; also known as sterol carrier protein 2 deficiency. LDMN is a syndrome characterized by leukoencephalopathy, dystonic head tremor, spasmodic torticollis and reduced tendon reflexes in lower extremities. Additional features include hyposmia, pathologic saccadic eye movements, a slight hypoacusis, accumulation of branched-chain pristanic acid in plasma, and the presence of abnormal bile alcohol glucuronides in urine.<ref>PMID:16685654</ref>
-==Function==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[http://www.uniprot.org/uniprot/NLTP_HUMAN NLTP_HUMAN]] Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis.<ref>PMID:8300590</ref><ref>PMID:17157249</ref>
+</div>
+== References ==
-==About this Structure==
+<references/>
-[[1qnd]] is a 1 chain structure with 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].
+__TOC__
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:010623549</ref><ref group="xtra">PMID:008243660</ref><references group="xtra"/><references/>
 [[Category: Homo sapiens]]
 [[Category: Choinowski, T.]]

1qnd: Difference between revisions

Revision as of 17:16, 29 September 2014

STEROL CARRIER PROTEIN-2, NMR, 20 STRUCTURES

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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