1av1: Difference between revisions
New page: left|200px<br /> <applet load="1av1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1av1, resolution 4.0Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1av1.gif|left|200px]]<br /> | [[Image:1av1.gif|left|200px]]<br /><applet load="1av1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1av1" size=" | |||
caption="1av1, resolution 4.0Å" /> | caption="1av1, resolution 4.0Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of truncated human apolipoprotein A-I (apo A-I), the major | The structure of truncated human apolipoprotein A-I (apo A-I), the major protein component of high density lipoprotein, has been determined at 4-A resolution. The crystals comprise residues 44-243 (exon 4) of apo A-I, a fragment that binds to lipid similarly to intact apo A-I and that retains the lipid-bound conformation even in the absence of lipid. The molecule consists almost entirely of a pseudo-continuous, amphipathic alpha-helix that is punctuated by kinks at regularly spaced proline residues; it adopts a shape similar to a horseshoe of dimensions 125 x 80 x 40 A. Four molecules in the asymmetric unit associate via their hydrophobic faces to form an antiparallel four-helix bundle with an elliptical ring shape. Based on this structure, we propose a model for the structure of apo A-I bound to high density lipoprotein. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1AV1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1AV1 is a [http://en.wikipedia.org/wiki/Single_protein 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=1AV1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Borhani, D | [[Category: Borhani, D W.]] | ||
[[Category: Brouillette, C | [[Category: Brouillette, C G.]] | ||
[[Category: Engler, J | [[Category: Engler, J A.]] | ||
[[Category: Rogers, D | [[Category: Rogers, D P.]] | ||
[[Category: atherosclerosis]] | [[Category: atherosclerosis]] | ||
[[Category: cholesterol metabolism]] | [[Category: cholesterol metabolism]] | ||
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[[Category: lipoprotein]] | [[Category: lipoprotein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:32 2008'' | ||
Revision as of 09:48, 21 February 2008
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CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I
Overview
The structure of truncated human apolipoprotein A-I (apo A-I), the major protein component of high density lipoprotein, has been determined at 4-A resolution. The crystals comprise residues 44-243 (exon 4) of apo A-I, a fragment that binds to lipid similarly to intact apo A-I and that retains the lipid-bound conformation even in the absence of lipid. The molecule consists almost entirely of a pseudo-continuous, amphipathic alpha-helix that is punctuated by kinks at regularly spaced proline residues; it adopts a shape similar to a horseshoe of dimensions 125 x 80 x 40 A. Four molecules in the asymmetric unit associate via their hydrophobic faces to form an antiparallel four-helix bundle with an elliptical ring shape. Based on this structure, we propose a model for the structure of apo A-I bound to high density lipoprotein.
Disease
Known diseases associated with this structure: Amyloidosis, 3 or more types OMIM:[107680], ApoA-I and apoC-III deficiency, combined OMIM:[107680], Corneal clouding, autosomal recessive OMIM:[107680], Hypertriglyceridemia, one form OMIM:[107680], Hypoalphalipoproteinemia OMIM:[107680]
About this Structure
1AV1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation., Borhani DW, Rogers DP, Engler JA, Brouillette CG, Proc Natl Acad Sci U S A. 1997 Nov 11;94(23):12291-6. PMID:9356442
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