TY - JOUR
T1 - Structural annotation of Beta-1,4-N-acetyl galactosaminyltransferase 1 (B4GALNT1) causing Hereditary Spastic Paraplegia 26
AU - Dad, Rubina
AU - Malik, Uzma
AU - Javed, Aneela
AU - Minassian, Berge A.
AU - Hassan, Muhammad Jawad
N1 - Funding Information:
Rubina Dad ( IRSIP 29 BMS 06 ) is partially supported by Higher Education Commission, Pakistan (HEC) for her PhD research. We are also grateful to our staff for coffee/tea during the course of manuscript assembly.
Publisher Copyright:
© 2017 Elsevier B.V.
PY - 2017/8/30
Y1 - 2017/8/30
N2 - Beta-1,4-N-acetyl galactosaminyltransferase 1, B4GALNT1, is a GM2/GD2 synthase, involved in the expression of glycosphingolipids (GSLs) containing sialic acid. Mutations in the gene B4GALNT1 cause Hereditary Spastic Paraplegia 26 (HSP26). In present study we have made attempt to predict the potential structural of the human B4GALNT1 protein. The results illustrated that the amino acid sequences of B4GALNT1 are not 100% conserved among selected twenty species. One signal peptide and one transmembrane domain predicted in human wild type B4GALNT1 protein with aliphatic index of 92.76 and theoretical (iso-electric point) pI of 8.93. It was a kind of unstable protein with Grand average of hydropathicity (GRAVY) of − 0.127. Various post-translational modifications were also predicted to exist in B4GALNT1 and predicted to interact with different proteins including ST8SIA5, SLC33A1, GLB1 and others. In the final round, reported missense mutations have shown the further decrease in stability of the protein. This in-silico analysis of B4GALNT1 protein will provide the basis for the further studies on structural variations and biological pathways involving B4GALNT1 in the HSP26.
AB - Beta-1,4-N-acetyl galactosaminyltransferase 1, B4GALNT1, is a GM2/GD2 synthase, involved in the expression of glycosphingolipids (GSLs) containing sialic acid. Mutations in the gene B4GALNT1 cause Hereditary Spastic Paraplegia 26 (HSP26). In present study we have made attempt to predict the potential structural of the human B4GALNT1 protein. The results illustrated that the amino acid sequences of B4GALNT1 are not 100% conserved among selected twenty species. One signal peptide and one transmembrane domain predicted in human wild type B4GALNT1 protein with aliphatic index of 92.76 and theoretical (iso-electric point) pI of 8.93. It was a kind of unstable protein with Grand average of hydropathicity (GRAVY) of − 0.127. Various post-translational modifications were also predicted to exist in B4GALNT1 and predicted to interact with different proteins including ST8SIA5, SLC33A1, GLB1 and others. In the final round, reported missense mutations have shown the further decrease in stability of the protein. This in-silico analysis of B4GALNT1 protein will provide the basis for the further studies on structural variations and biological pathways involving B4GALNT1 in the HSP26.
KW - 3-D structure of B4galnt1
KW - B4GALNT1
KW - Bioinformatics tools
KW - HSP26
KW - Structural insights
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U2 - 10.1016/j.gene.2017.05.041
DO - 10.1016/j.gene.2017.05.041
M3 - Article
C2 - 28536081
AN - SCOPUS:85028503250
SN - 0378-1119
VL - 626
SP - 258
EP - 263
JO - Gene
JF - Gene
ER -