Protein-oligosaccharide interaction mechanisms in chitinases engineered towards neolectins

Research output: Contribution to journalOther journal contributionScientificpeer-review

Abstract

Speciſc protein-carbohydrate interactions are fundamental to many biomolecular recognition events. The study concentrates on fungal 42kDa chitinase from Trichoderma harzianum, a naturally chitin (polymer of N-acetylglucosamine residues) degrading enzyme. It has shown activity also on synthetically modiſed D-1,3- fucosylated and E-1,4-galactosylated, more animal type of chitooligosaccharides. The structure of chitinase (D/E-barrel fold) with the substrate binding cleft formed by limited number of loops provides an excellent platform for directed evolution studies. In this study our aim is to obtain atomic level understanding of the factors determining the interactions between an oligosaccharide and a protein by using molecular dynamic simulations. The results from modeling are compared with the experimental data (mutagenesis, mass spectroscopy and nuclear magnetic resonance). The computational studies with the experimental work aim at development of neolectins, i.e. proteins selectively binding to given, medically important, oligosaccharide structures, achieved by ſrst deactivating and then engineering fungal chitinases towards the desired speciſcity and afſnity.
Original languageEnglish
Article numberP-626
Pages (from-to)741
Number of pages1
JournalEuropean Biophysics Journal
Volume34
Issue number6
DOIs
Publication statusPublished - 2005
MoE publication typeA1 Journal article-refereed
Event5th European Biophysics Congress - Montpellier, France
Duration: 27 Aug 20051 Sep 2005

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Chitinases
Oligosaccharides
Proteins
Trichoderma
Chitin
Acetylglucosamine
Molecular Dynamics Simulation
Protein Binding
Mutagenesis
Mass Spectrometry
Polymers
Magnetic Resonance Spectroscopy
Carbohydrates
Enzymes

Cite this

@article{ec525fb716c342a2ad511496344f36b3,
title = "Protein-oligosaccharide interaction mechanisms in chitinases engineered towards neolectins",
abstract = "Speciſc protein-carbohydrate interactions are fundamental to many biomolecular recognition events. The study concentrates on fungal 42kDa chitinase from Trichoderma harzianum, a naturally chitin (polymer of N-acetylglucosamine residues) degrading enzyme. It has shown activity also on synthetically modiſed D-1,3- fucosylated and E-1,4-galactosylated, more animal type of chitooligosaccharides. The structure of chitinase (D/E-barrel fold) with the substrate binding cleft formed by limited number of loops provides an excellent platform for directed evolution studies. In this study our aim is to obtain atomic level understanding of the factors determining the interactions between an oligosaccharide and a protein by using molecular dynamic simulations. The results from modeling are compared with the experimental data (mutagenesis, mass spectroscopy and nuclear magnetic resonance). The computational studies with the experimental work aim at development of neolectins, i.e. proteins selectively binding to given, medically important, oligosaccharide structures, achieved by ſrst deactivating and then engineering fungal chitinases towards the desired speciſcity and afſnity.",
author = "Nana Munck and Kirsi Tappura and Olli Aitio and Hannu Maaheimo and Harry Boer and Anu Koivula",
note = "Poster abstract P-626",
year = "2005",
doi = "10.1007/s00249-005-0503-y",
language = "English",
volume = "34",
pages = "741",
journal = "European Biophysics Journal",
issn = "0175-7571",
publisher = "Springer",
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}

Protein-oligosaccharide interaction mechanisms in chitinases engineered towards neolectins. / Munck, Nana; Tappura, Kirsi; Aitio, Olli; Maaheimo, Hannu; Boer, Harry; Koivula, Anu.

In: European Biophysics Journal, Vol. 34, No. 6, P-626, 2005, p. 741.

Research output: Contribution to journalOther journal contributionScientificpeer-review

TY - JOUR

T1 - Protein-oligosaccharide interaction mechanisms in chitinases engineered towards neolectins

AU - Munck, Nana

AU - Tappura, Kirsi

AU - Aitio, Olli

AU - Maaheimo, Hannu

AU - Boer, Harry

AU - Koivula, Anu

N1 - Poster abstract P-626

PY - 2005

Y1 - 2005

N2 - Speciſc protein-carbohydrate interactions are fundamental to many biomolecular recognition events. The study concentrates on fungal 42kDa chitinase from Trichoderma harzianum, a naturally chitin (polymer of N-acetylglucosamine residues) degrading enzyme. It has shown activity also on synthetically modiſed D-1,3- fucosylated and E-1,4-galactosylated, more animal type of chitooligosaccharides. The structure of chitinase (D/E-barrel fold) with the substrate binding cleft formed by limited number of loops provides an excellent platform for directed evolution studies. In this study our aim is to obtain atomic level understanding of the factors determining the interactions between an oligosaccharide and a protein by using molecular dynamic simulations. The results from modeling are compared with the experimental data (mutagenesis, mass spectroscopy and nuclear magnetic resonance). The computational studies with the experimental work aim at development of neolectins, i.e. proteins selectively binding to given, medically important, oligosaccharide structures, achieved by ſrst deactivating and then engineering fungal chitinases towards the desired speciſcity and afſnity.

AB - Speciſc protein-carbohydrate interactions are fundamental to many biomolecular recognition events. The study concentrates on fungal 42kDa chitinase from Trichoderma harzianum, a naturally chitin (polymer of N-acetylglucosamine residues) degrading enzyme. It has shown activity also on synthetically modiſed D-1,3- fucosylated and E-1,4-galactosylated, more animal type of chitooligosaccharides. The structure of chitinase (D/E-barrel fold) with the substrate binding cleft formed by limited number of loops provides an excellent platform for directed evolution studies. In this study our aim is to obtain atomic level understanding of the factors determining the interactions between an oligosaccharide and a protein by using molecular dynamic simulations. The results from modeling are compared with the experimental data (mutagenesis, mass spectroscopy and nuclear magnetic resonance). The computational studies with the experimental work aim at development of neolectins, i.e. proteins selectively binding to given, medically important, oligosaccharide structures, achieved by ſrst deactivating and then engineering fungal chitinases towards the desired speciſcity and afſnity.

U2 - 10.1007/s00249-005-0503-y

DO - 10.1007/s00249-005-0503-y

M3 - Other journal contribution

VL - 34

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JO - European Biophysics Journal

JF - European Biophysics Journal

SN - 0175-7571

IS - 6

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ER -