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1av1
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1av1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1av1 OCA], [http://www.ebi.ac.uk/pdbsum/1av1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1av1 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107680 107680]], ApoA-I and apoC-III deficiency, combined OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107680 107680]], Corneal clouding, autosomal recessive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107680 107680]], Hypertriglyceridemia, one form OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107680 107680]], Hypoalphalipoproteinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107680 107680]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: lipoprotein]] | [[Category: lipoprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:01 2008'' |
Revision as of 15:48, 30 March 2008
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| , resolution 4.0Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
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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