Three-Dimensional Models of the Oligomeric Human Asialoglycoprotein Receptor (ASGP-R)

The work presented here is aimed at suggesting plausible hypotheses for functional oligomeric forms of the human asialoglycoprotein receptor (ASGP-R), by applying a combination of different computational techniques. The functional ASGP-R is a hetero-oligomer, that comprises of several subunits of tw...

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Main Authors: Anna Maria Bianucci, Ilaria Massarelli, Federica Chiellini, Emo Chiellini
Format: Article
Language:English
Published: MDPI AG 2010-10-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:http://www.mdpi.com/1422-0067/11/10/3867/
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spelling doaj-b8d86ff86644424f812b367ac4a4f24c2020-11-24T22:01:01ZengMDPI AGInternational Journal of Molecular Sciences1422-00672010-10-0111103867388410.3390/ijms11103867Three-Dimensional Models of the Oligomeric Human Asialoglycoprotein Receptor (ASGP-R)Anna Maria BianucciIlaria MassarelliFederica ChielliniEmo ChielliniThe work presented here is aimed at suggesting plausible hypotheses for functional oligomeric forms of the human asialoglycoprotein receptor (ASGP-R), by applying a combination of different computational techniques. The functional ASGP-R is a hetero-oligomer, that comprises of several subunits of two different kinds (H1 and H2), which are highly homologous. Its stoichiometry is still unknown. An articulated step-wise modeling protocol was used in order to build the receptor model in a minimal oligomeric form, necessary for it to bind multi-antennary carbohydrate ligands. The ultimate target of the study is to contribute to increasing the knowledge of interactions between the human ASGP-R and carbohydrate ligands, at the molecular level, pertinent to applications in the field of hepatic tissue engineering. http://www.mdpi.com/1422-0067/11/10/3867/ASGP-Roligomeric formantennary carbohydratic ligands
collection DOAJ
language English
format Article
sources DOAJ
author Anna Maria Bianucci
Ilaria Massarelli
Federica Chiellini
Emo Chiellini
spellingShingle Anna Maria Bianucci
Ilaria Massarelli
Federica Chiellini
Emo Chiellini
Three-Dimensional Models of the Oligomeric Human Asialoglycoprotein Receptor (ASGP-R)
International Journal of Molecular Sciences
ASGP-R
oligomeric form
antennary carbohydratic ligands
author_facet Anna Maria Bianucci
Ilaria Massarelli
Federica Chiellini
Emo Chiellini
author_sort Anna Maria Bianucci
title Three-Dimensional Models of the Oligomeric Human Asialoglycoprotein Receptor (ASGP-R)
title_short Three-Dimensional Models of the Oligomeric Human Asialoglycoprotein Receptor (ASGP-R)
title_full Three-Dimensional Models of the Oligomeric Human Asialoglycoprotein Receptor (ASGP-R)
title_fullStr Three-Dimensional Models of the Oligomeric Human Asialoglycoprotein Receptor (ASGP-R)
title_full_unstemmed Three-Dimensional Models of the Oligomeric Human Asialoglycoprotein Receptor (ASGP-R)
title_sort three-dimensional models of the oligomeric human asialoglycoprotein receptor (asgp-r)
publisher MDPI AG
series International Journal of Molecular Sciences
issn 1422-0067
publishDate 2010-10-01
description The work presented here is aimed at suggesting plausible hypotheses for functional oligomeric forms of the human asialoglycoprotein receptor (ASGP-R), by applying a combination of different computational techniques. The functional ASGP-R is a hetero-oligomer, that comprises of several subunits of two different kinds (H1 and H2), which are highly homologous. Its stoichiometry is still unknown. An articulated step-wise modeling protocol was used in order to build the receptor model in a minimal oligomeric form, necessary for it to bind multi-antennary carbohydrate ligands. The ultimate target of the study is to contribute to increasing the knowledge of interactions between the human ASGP-R and carbohydrate ligands, at the molecular level, pertinent to applications in the field of hepatic tissue engineering.
topic ASGP-R
oligomeric form
antennary carbohydratic ligands
url http://www.mdpi.com/1422-0067/11/10/3867/
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