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Rapid folding and unfolding of Apaf-1 CARD.

Abstract：

:Caspase recruitment domains (CARDs) are members of the death domain superfamily and contain six antiparallel helices in an alpha-helical Greek key topology. We have examined the equilibrium and kinetic folding of the CARD of Apaf-1 (apoptotic protease activating factor 1), which consists of 97 amino acid residues, at pH 6 and pH 8. The results showed that an apparent two state equilibrium mechanism is not adequate to describe the folding of Apaf-1 CARD at either pH, suggesting the presence of intermediates in equilibrium unfolding. Interestingly, the results showed that the secondary structure is less stable than the tertiary structure, based on the transition mid-points for unfolding. Single mixing and sequential mixing stopped-flow studies showed that Apaf-1 CARD folds and unfolds rapidly and suggest a folding mechanism that contains parallel channels with two unfolded conformations folding to the native conformation. Kinetic simulations show that a slow folding phase is described by a third conformation in the unfolded ensemble that interconverts with one or both unfolded species. Overall, the native ensemble is formed rapidly upon refolding. This is in contrast to other CARDs in which folding appears to be dominated by formation of kinetic traps.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Milam SL,Nicely NI,Feeney B,Mattos C,Clark AC

doi

10.1016/j.jmb.2007.02.105

subject

Has Abstract

pub_date

2007-05-25 00:00:00

pages

290-304

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(07)00291-4

journal_volume

369

pub_type

杂志文章

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