PMID: 9650076Jul 3, 1998Paper

alpha-Crystallin C-terminal domain: on the track of an Ig fold

International Journal of Biological Macromolecules
J P MornonA Tardieu

Abstract

New results obtained from a two-dimensional sequence analysis of the small heat shock protein (shsp) family are described. It is confirmed that the conserved C-terminal alpha-crystallin domain is essentially made of beta-strands, most probably two groups of beta-strands separated by a large loop. A direct correspondence between the putative beta-strands that have been identified in shsps and the seven beta-strands of a classical immunoglobulin-like fold is proposed. The hypothesis that the shsp family could belong to the immunoglobulin superfamily (IgSF) is consistent with the ubiquitous distribution and the multifunctional properties of the crystallins that are now emerging.

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Citations

Dec 14, 2001·Biochemical and Biophysical Research Communications·Q Mao, Z Chang
Jun 22, 2005·Journal of Molecular Biology·Titus M FranzmannJohannes Buchner
Aug 11, 2004·Progress in Biophysics and Molecular Biology·Hans BloemendalAnnette Tardieu
May 2, 2014·Journal of Controlled Release : Official Journal of the Controlled Release Society·Wan WangJ Andrew MacKay
Aug 6, 1999·Protein Engineering·D M HalabyJ Mornon
Dec 4, 2004·Clinical & Experimental Optometry : Journal of the Australian Optometrical Association·Robert C Augusteyn
Jan 11, 2000·Eye·C Slingsby, N J Clout
Mar 30, 2001·The Journal of Biological Chemistry·I K FeilD I Svergun
Dec 17, 2003·The Journal of Biological Chemistry·Belinda BullardWolfgang A Linke
Dec 6, 2020·International Journal of Biological Macromolecules·Ajamaluddin MalikMohammad Z Ahmed
Mar 29, 2000·Seminars in Cell & Developmental Biology·J Horwitz
Jul 17, 1999·Biochimica Et Biophysica Acta·M BloemendalW C Johnson

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