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| - | [[Image:2a01.gif|left|200px]]
| + | <span style='background-color: yellow;'>For additional information see '''2009, December:''' at [[Retractions and Fraud]].</span></br>REMOVED: The PDB entry 2a01 was removed. |
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| - | {{Structure
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| - | |PDB= 2a01 |SIZE=350|CAPTION= <scene name='initialview01'>2a01</scene>, resolution 2.40Å
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| - | |SITE=
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| - | |LIGAND= <scene name='pdbligand=AC9:TRISACETYLACETONATOCHROMIUM(III)'>AC9</scene>
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| - | |ACTIVITY=
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| - | |GENE=
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| - | |DOMAIN=
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| - | |RELATEDENTRY=
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| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a01 OCA], [http://www.ebi.ac.uk/pdbsum/2a01 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a01 RCSB]</span>
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| - | }}
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| - | '''Crystal Structure of Lipid-free Human Apolipoprotein A-I''' | + | |
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| - | ==Overview==
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| - | Despite three decades of extensive studies on human apolipoprotein A-I (apoA-I), the major protein component in high-density lipoproteins, the molecular basis for its antiatherogenic function is elusive, in part because of lack of a structure of the full-length protein. We describe here the crystal structure of lipid-free apoA-I at 2.4 A. The structure shows that apoA-I is comprised of an N-terminal four-helix bundle and two C-terminal helices. The N-terminal domain plays a prominent role in maintaining its lipid-free conformation, indicating that mutants with truncations in this region form inadequate models for explaining functional properties of apoA-I. A model for transformation of the lipid-free conformation to the high-density lipoprotein-bound form follows from an analysis of solvent-accessible hydrophobic patches on the surface of the structure and their proximity to the hydrophobic core of the four-helix bundle. The crystal structure of human apoA-I displays a hitherto-unobserved array of positively and negatively charged areas on the surface. Positioning of the charged surface patches relative to hydrophobic regions near the C terminus of the protein offers insights into its interaction with cell-surface components of the reverse cholesterol transport pathway and antiatherogenic properties of this protein. This structure provides a much-needed structural template for exploration of molecular mechanisms by which human apoA-I ameliorates atherosclerosis and inflammatory diseases.
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| - | ==About this Structure==
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| - | 2A01 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A01 OCA].
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| - | ==Reference==
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| - | Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases., Ajees AA, Anantharamaiah GM, Mishra VK, Hussain MM, Murthy HM, Proc Natl Acad Sci U S A. 2006 Feb 14;103(7):2126-31. Epub 2006 Feb 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16452169 16452169]
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| - | [[Category: Homo sapiens]]
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| - | [[Category: Single protein]]
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| - | [[Category: Ajees, A A.]]
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| - | [[Category: Anantharamaiah, G M.]]
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| - | [[Category: Hussain, M M.]]
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| - | [[Category: Mishra, V K.]]
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| - | [[Category: Murthy, K H.M.]]
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| - | [[Category: four-helix bundle]]
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:46:05 2008''
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