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Titolo:
MOLECULAR MODELING OF VIMENTIN FILAMENT ASSEMBLY
Autore:
DOWNING DT;
Indirizzi:
UNIV IOWA,COLL MED,MED LABS 270,DEPT DERMATOL,MARSHALL RES LABS IOWA CITY IA 52242
Titolo Testata:
Proteins
fascicolo: 4, volume: 26, anno: 1996,
pagine: 472 - 478
SICI:
0887-3585(1996)26:4<472:MMOVFA>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
1/KERATIN-10 INTERMEDIATE FILAMENTS; COILED-COIL MOLECULES; PROTOFILAMENT UNIT; CROSS-LINKING; PROTEINS; MECHANISM; INVITRO;
Keywords:
VIMENTIN; DESMIN; KERATIN; ALPHA HELIX; BETA HELIX; BETA STRAND; COILED COIL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
18
Recensione:
Indirizzi per estratti:
Citazione:
D.T. Downing, "MOLECULAR MODELING OF VIMENTIN FILAMENT ASSEMBLY", Proteins, 26(4), 1996, pp. 472-478

Abstract

Intermediate-filament forming proteins are known to form rod-shaped dimers that are calculated to be 45 nn in length. Molecular modeling indicates that the dimerization is promoted by interchain hydrophobic interactions between sections of (alpha helix and beta helix. Further aggregation involves the formation of tetramers in which two dimers are antiparallel and staggered to two characteristic degrees of overlap. Modeling indicated that the degrees of stagger are dictated by the association of sections of alpha helix in 4-chain bundles, in which hydrophobic side chains are sequestered from contact with water. The staggered arrangement of two dimers produces a tetramer having sections of 2-chain rod in which hydrophobic side chains are exposed to water. Extension of the tetramer to form protofilaments may be driven by associations with the 2-chain regions that reduce aqueous exposure of the hydrophobic side chains. Exposure of hydrophobic groups may be reduced by the 2-chain regions folding back upon themselves so that the entire tetramer becomes a 4-chain conformation. This prediction is in line with electron microscope data showing that mixtures of the lower oligomers contain rods of uniform thickness ranging upwards from 45 nm in a series having incremental increases in length. Data from previous chemicalcrosslinking studies support this model and also the idea that the completed intermediate filaments each consist of seven 4-chain protofilaments. (C) 1996 Wiley-Liss Inc.

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Documento generato il 25/09/20 alle ore 00:34:39