Fold-recognition and comparative modeling of human α2,3-sialyltransferases reveal their sequence and structural similarities to CstII from Campylobacter jejuni

Table 1 Accession numbers and modelled regions of human SiaTs

Name	NCBI accession number	Length (number of residues)	Transmembrane domain^¶	Modeled region^§	Reference
ST3Gal I	AAA36612	340	12–35	66–332	[63]
ST3Gal II	NP_008858	350	7–29	76–347	[64]
ST3Gal III	AAA35778	375	4–26	92–369	[65]
ST3Gal IV	AAA16460	332	5–20	51–329	[66]
ST3Gal V	Q9UNP4	362	15–32	70–354	[67]
ST3Gal VI	Q9Y274	331	10–32	51–323	[19]

^¶Predicted using the TMHMM server [42].
^§All the residues of the protein except those in the N-terminal cytoplasmic, transmembrane domains and last few residues of the catalytic region were considered for 3-D structure modeling. However, part of the neck/stem region could not be modeled for reasons detailed in the text.

ISSN: 1472-6807