Fold-recognition and comparative modeling of human alpha2,3-sialyltransferases reveal their sequence and structural similarities to CstII from Campylobacter jejuni.

ABSTRACT:

Background

The 3-D structure of none of the eukaryotic sialyltransferases (SiaTs) has been determined so far. Sequence alignment algorithms such as BLAST and PSI-BLAST could not detect a homolog of these enzymes from the protein databank. SiaTs, thus, belong to the hard/medium target category in the CASP experiments. The objective of the current work is to model the 3-D structures of human SiaTs which transfer the sialic acid in alpha2,3-linkage viz., ST3Gal I, II, III, IV, V, and VI, using fold-recognition and comparative modeling methods. The pair-wise sequence similarity among these six enzymes ranges from 41 to 63%.

Results

Unlike the sequence similarity servers, fold-recognition servers identified CstII, a alpha2,3/8 dual-activity SiaT from Campylobacter jejuni as the h

SUBMITTER: Sujatha MS 

PROVIDER: S-EPMC1508147 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature