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Determining the 3D structure of human ASC2 protein involved in apoptosis and inflammation.

Abstract：

:ASC2 structure has been well defined by 1141 NOE experimental restraints. The model consists of five alpha helices. alpha-Helices are connected by short random structure loops. The sole exception is the loop connecting helices 2 and 3, which has a 20-residue length. Folding generally agrees with the folding of recently published death domain structures in which alpha-helix structures have been reported. In spite of structural similarity, amino acid sequence homology with the most similar protein (ASC1) is just 64%. DD, DED, and CASP protein structures present six helices along their sequences; ASC2 presents 5 well-defined helices due to long distance restraints. However, a helical fragment was observed between amino acids 38 and 42 (representing helix 3) in the death domains when constructing the model.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Espejo F,Patarroyo ME

doi

10.1016/j.bbrc.2005.12.087

subject

Has Abstract

pub_date

2006-02-17 00:00:00

pages

860-4

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)02835-4

journal_volume

340

pub_type

杂志文章

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