1av1
From Proteopedia
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| - | [[Image:1av1.gif|left|200px]] | + | [[Image:1av1.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I''' | + | {{Structure |
| + | |PDB= 1av1 |SIZE=350|CAPTION= <scene name='initialview01'>1av1</scene>, resolution 4.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AV1 is a [ | + | 1AV1 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=1AV1 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9356442 9356442] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lipoprotein]] | [[Category: lipoprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:37 2008'' |
Revision as of 08:02, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I
Contents |
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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