In silico modeling of lipase H

Amara Jabeen, Asif Mir, Jabar Zaman Khan Khattak, Naveeda Riaz

Research output: Contribution to journalArticleResearchpeer-review

Abstract

LAH 2 is a type of autosomal recessive hypotrichosis that affect hairs, eyebrows, scalp and eyelashes. Mutations in Lipase H gene result in LAH 2. Changes that result from mutation on physiochemical properties, post-translational modifications, functional sites, secondary structure and tertiary structure lipase H gene (LIPH) at molecular level were analyzed in the current study. Results indicate that the 3rd motif of LIPH deletes as a result of mutation. The number of alpha helices and beta sheets become varied in normal and abnormal protein. Tertiary structure of LIPH was predicted through homology modeling. Mutations were then inserted to reveal the difference between normal and abnormal structure. Ligands to target LIPH are also retrieved. ASP178, ASP207 and HIS248 constitute the active site of LIPH. Missense mutations in LIPH also brought drastic changes at molecular level that led to imbalanced function. All these changes can be studied through bioinformatics without going for expensive laborious and time consuming experimental techniques.
LanguageEnglish
Pages2051-2057
Number of pages7
JournalAfrican Journal of Biotechnology
Volume12
Issue number16
DOIs
Publication statusPublished - 17 Apr 2013
Externally publishedYes

Fingerprint

Lipase
Computer Simulation
Genes
genes
mutation
Mutation
Eyelashes
Eyebrows
missense mutation
post-translational modification
Missense Mutation
Post Translational Protein Processing
Computational Biology
Scalp
bioinformatics
active sites
hairs
Catalytic Domain
Ligands
Proteins

Bibliographical note

Copyright the Author(s) 2018. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

Keywords

  • LAH2
  • LIPH
  • tertiary structure
  • secondary structure
  • physiochemical properties
  • ligands
  • active site

Cite this

Jabeen, A., Mir, A., Khattak, J. Z. K., & Riaz, N. (2013). In silico modeling of lipase H. African Journal of Biotechnology, 12(16), 2051-2057. https://doi.org/10.5897/AJB10.1032
Jabeen, Amara ; Mir, Asif ; Khattak, Jabar Zaman Khan ; Riaz, Naveeda. / In silico modeling of lipase H. In: African Journal of Biotechnology. 2013 ; Vol. 12, No. 16. pp. 2051-2057.
@article{d47469a6aa59461e9bd8950f1b6b15c3,
title = "In silico modeling of lipase H",
abstract = "LAH 2 is a type of autosomal recessive hypotrichosis that affect hairs, eyebrows, scalp and eyelashes. Mutations in Lipase H gene result in LAH 2. Changes that result from mutation on physiochemical properties, post-translational modifications, functional sites, secondary structure and tertiary structure lipase H gene (LIPH) at molecular level were analyzed in the current study. Results indicate that the 3rd motif of LIPH deletes as a result of mutation. The number of alpha helices and beta sheets become varied in normal and abnormal protein. Tertiary structure of LIPH was predicted through homology modeling. Mutations were then inserted to reveal the difference between normal and abnormal structure. Ligands to target LIPH are also retrieved. ASP178, ASP207 and HIS248 constitute the active site of LIPH. Missense mutations in LIPH also brought drastic changes at molecular level that led to imbalanced function. All these changes can be studied through bioinformatics without going for expensive laborious and time consuming experimental techniques.",
keywords = "LAH2, LIPH, tertiary structure, secondary structure, physiochemical properties, ligands, active site",
author = "Amara Jabeen and Asif Mir and Khattak, {Jabar Zaman Khan} and Naveeda Riaz",
note = "Copyright the Author(s) 2018. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.",
year = "2013",
month = "4",
day = "17",
doi = "10.5897/AJB10.1032",
language = "English",
volume = "12",
pages = "2051--2057",
journal = "African Journal of Biotechnology",
issn = "1684-5315",
publisher = "Academic Journals",
number = "16",

}

Jabeen, A, Mir, A, Khattak, JZK & Riaz, N 2013, 'In silico modeling of lipase H', African Journal of Biotechnology, vol. 12, no. 16, pp. 2051-2057. https://doi.org/10.5897/AJB10.1032

In silico modeling of lipase H. / Jabeen, Amara; Mir, Asif; Khattak, Jabar Zaman Khan; Riaz, Naveeda.

In: African Journal of Biotechnology, Vol. 12, No. 16, 17.04.2013, p. 2051-2057.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - In silico modeling of lipase H

AU - Jabeen, Amara

AU - Mir, Asif

AU - Khattak, Jabar Zaman Khan

AU - Riaz, Naveeda

N1 - Copyright the Author(s) 2018. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

PY - 2013/4/17

Y1 - 2013/4/17

N2 - LAH 2 is a type of autosomal recessive hypotrichosis that affect hairs, eyebrows, scalp and eyelashes. Mutations in Lipase H gene result in LAH 2. Changes that result from mutation on physiochemical properties, post-translational modifications, functional sites, secondary structure and tertiary structure lipase H gene (LIPH) at molecular level were analyzed in the current study. Results indicate that the 3rd motif of LIPH deletes as a result of mutation. The number of alpha helices and beta sheets become varied in normal and abnormal protein. Tertiary structure of LIPH was predicted through homology modeling. Mutations were then inserted to reveal the difference between normal and abnormal structure. Ligands to target LIPH are also retrieved. ASP178, ASP207 and HIS248 constitute the active site of LIPH. Missense mutations in LIPH also brought drastic changes at molecular level that led to imbalanced function. All these changes can be studied through bioinformatics without going for expensive laborious and time consuming experimental techniques.

AB - LAH 2 is a type of autosomal recessive hypotrichosis that affect hairs, eyebrows, scalp and eyelashes. Mutations in Lipase H gene result in LAH 2. Changes that result from mutation on physiochemical properties, post-translational modifications, functional sites, secondary structure and tertiary structure lipase H gene (LIPH) at molecular level were analyzed in the current study. Results indicate that the 3rd motif of LIPH deletes as a result of mutation. The number of alpha helices and beta sheets become varied in normal and abnormal protein. Tertiary structure of LIPH was predicted through homology modeling. Mutations were then inserted to reveal the difference between normal and abnormal structure. Ligands to target LIPH are also retrieved. ASP178, ASP207 and HIS248 constitute the active site of LIPH. Missense mutations in LIPH also brought drastic changes at molecular level that led to imbalanced function. All these changes can be studied through bioinformatics without going for expensive laborious and time consuming experimental techniques.

KW - LAH2

KW - LIPH

KW - tertiary structure

KW - secondary structure

KW - physiochemical properties

KW - ligands

KW - active site

U2 - 10.5897/AJB10.1032

DO - 10.5897/AJB10.1032

M3 - Article

VL - 12

SP - 2051

EP - 2057

JO - African Journal of Biotechnology

T2 - African Journal of Biotechnology

JF - African Journal of Biotechnology

SN - 1684-5315

IS - 16

ER -