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Titolo:
Crystallization of truncated human apolipoprotein A-I in a novel conformation
Autore:
Borhani, DW; Engler, JA; Brouillette, CG;
Indirizzi:
So Res Inst, Dept Organ Chem, Birmingham, AL 35205 USA So Res Inst Birmingham AL USA 35205 Organ Chem, Birmingham, AL 35205 USA Univ Alabama, Med Ctr, Dept Biochem & Mol Genet, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Mol Genet, Birmingham, AL 35294 USA Univ Alabama, Med Ctr, Ctr Macromol Crystallog, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Crystallog, Birmingham, AL 35294 USA
Titolo Testata:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
, volume: 55, anno: 1999,
parte:, 9
pagine: 1578 - 1583
SICI:
0907-4449(199909)55:<1578:COTHAA>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
HIGH-DENSITY-LIPOPROTEIN; CORONARY HEART-DISEASE; LIPID-FREE STRUCTURE; TERMINAL DELETIONS; CHOLESTEROL LEVELS; TRANSGENIC MICE; HDL; FRAMINGHAM; PROTEINS; MODELS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Borhani, DW So Res Inst, Dept Organ Chem, Birmingham, AL 35205 USA So Res Inst Birmingham AL USA 35205 Birmingham, AL 35205 USA
Citazione:
D.W. Borhani et al., "Crystallization of truncated human apolipoprotein A-I in a novel conformation", ACT CRYST D, 55, 1999, pp. 1578-1583

Abstract

The crystallization of recombinant human apolipoprotein A-I (apo A-I), themajor protein component of high-density lipoprotein, in a new crystal formis described, The fragment crystallized, residues 44-243 of native apo A-I[apo Delta(1-43)A-I], is very similar to intact native apo A-I in its ability to bind lipid, to be incorporated into high-density lipoproteins and toactivate lecithin-cholesterol acyl transferase, Apo a(1-43)A-I crystallizes, in the presence of beta-D-octylglucopyranoside, in space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 37.11, b = 123.62, c = 164.65 Angstrom and a diffraction limit of 3.2 Angstrom These form II crystals growunder conditions of significantly lower ionic strength than the original form I crystals (space group P2(1)2(1)2(1), a = 97.47, b = 113.87, c = 196.19 Angstrom, diffraction limit 3.0 Angstrom). Packing arguments show that the unusual open conformation of apo a(1-43)A-I found in the form I crystals cannot be packed into the smaller oddly proportioned form IZ unit cell, Monomeric apo Delta(1-43)A-I, as either a four-helix bundle (similar to 75 x 30 x 30 A) or an extended helical rod (similar to 150 x 20 x 20 Angstrom), can be packed into the form II unit cell. It is concluded, therefore, that ape Delta(1-43)A-I may have crystallized in one of these distinct conformations in the form II crystals.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 19:49:30