Influence of Trp flipping on carbohydrate binding in lectins.
An example on Aleuria aurantia lectin AAL

J 2017

Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL

HOUSER, Josef, Stanislav KOZMON, Deepti MISHRA, Sushil Kumar MISHRA, Patrick R ROMANO et. al.

Basic information

Original name

Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL

Authors

HOUSER, Josef (203 Czech Republic, belonging to the institution), Stanislav KOZMON (703 Slovakia, belonging to the institution), Deepti MISHRA (356 India, belonging to the institution), Sushil Kumar MISHRA (356 India, belonging to the institution), Patrick R ROMANO (840 United States of America), Michaela WIMMEROVÁ (203 Czech Republic, belonging to the institution) and Jaroslav KOČA (203 Czech Republic, guarantor, belonging to the institution)

Edition

Plos one, San Francisco, Public Library of Science, 2017, 1932-6203

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 2.766

RIV identification code

RIV/00216224:14740/17:00095446

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1371/journal.pone.0189375

UT WoS

000417698200036

Keywords in English

FUCOSE-SPECIFIC LECTIN; DISPERSION INTERACTIONS; CRYSTAL-STRUCTURE; PI INTERACTION; CORE FUCOSE; PROTEIN; APPROXIMATION; ENERGY; RECOGNITION; SPECIFICITY

Abstract

ORIG CZ

V originále

Protein-carbohydrate interactions are very often mediated by the stacking CH-pi interactions involving the side chains of aromatic amino acids such as tryptophan (Trp), tyrosine (Tyr) or phenylalanine (Phe). Especially suitable for stacking is the Trp residue. Analysis of the PDB database shows Trp stacking for 265 carbohydrate or carbohydrate-like ligands in 5 208 Trp-containing motives. An appropriate model system to study such an interaction is the AAL lectin family, where the stacking interactions play a crucial role and are thought to be a driving force for carbohydrate binding. In this study we present data showing a novel finding in the stacking interaction of the AAL Trp side chain with the carbohydrate. High resolution X-ray structure of the AAL lectin from Aleuria aurantia with alpha-methyl-L-fucoside ligand shows two possible Trp side chain conformations with the same occupation in electron density. The in silico data shows that the conformation of the Trp side chain does not influence the interaction energy despite the fact that each conformation creates interactions with different carbohydrate CH groups. Moreover, the PDB data search shows that the conformations are almost equally distributed across all Trp-carbohydrate complexes, which would suggest no substantial preference for one conformation over another.

In Czech

Interakce protein-cukr jsou často zprostředkovány pomocí CH-pi interakce zahrnující boční řetězec aromatické aminokyseliny. Analýza PDB databáze prokázala tuto interakci pro 265 ligandů a 5208 motivů. Modelový systém interakce je lektinová rodina AAL. V této studii jsme pomocí RTG struktury s vysokým rozlišením a následné in silico analýze prokázali existenci dvou preferovaných konformerů Trp a porovnali jejich výskyt a energetickou bilanci pro vazbu sacharidu.

Links

GA13-25401S, research and development project

Name: Studium proteinů z patogenů zapojených do rozpoznávání hostitelského organismu

Investor: Czech Science Foundation

LM2015085, research and development project

Name: CERIT Scientific Cloud (Acronym: CERIT-SC)

Investor: Ministry of Education, Youth and Sports of the CR, CERIT Scientific Cloud

LQ1601, research and development project

Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

HOUSER, Josef, Stanislav KOZMON, Deepti MISHRA, Sushil Kumar MISHRA, Patrick R ROMANO, Michaela WIMMEROVÁ and Jaroslav KOČA. Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL. Plos one. San Francisco: Public Library of Science, 2017, vol. 12, No 12, p. 0189375-189391. ISSN 1932-6203. Available from: https://dx.doi.org/10.1371/journal.pone.0189375.

@article{1405370,
   author = {Houser, Josef and Kozmon, Stanislav and Mishra, Deepti and Mishra, Sushil Kumar and Romano, Patrick R and Wimmerová, Michaela and Koča, Jaroslav},
   article_location = {San Francisco},
   article_number = {12},
   doi = {http://dx.doi.org/10.1371/journal.pone.0189375},
   keywords = {FUCOSE-SPECIFIC LECTIN; DISPERSION INTERACTIONS; CRYSTAL-STRUCTURE; PI INTERACTION; CORE FUCOSE; PROTEIN; APPROXIMATION; ENERGY; RECOGNITION; SPECIFICITY},
   language = {eng},
   issn = {1932-6203},
   journal = {Plos one},
   title = {Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL},
   url = {http://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0189375&type=printable},
   volume = {12},
   year = {2017}
}

TY  - JOUR
ID  - 1405370
AU  - Houser, Josef - Kozmon, Stanislav - Mishra, Deepti - Mishra, Sushil Kumar - Romano, Patrick R - Wimmerová, Michaela - Koča, Jaroslav
PY  - 2017
TI  - Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL
JF  - Plos one
VL  - 12
IS  - 12
SP  - 0189375
EP  - 0189375
PB  - Public Library of Science
SN  - 19326203
KW  - FUCOSE-SPECIFIC LECTIN
KW  - DISPERSION INTERACTIONS
KW  - CRYSTAL-STRUCTURE
KW  - PI INTERACTION
KW  - CORE FUCOSE
KW  - PROTEIN
KW  - APPROXIMATION
KW  - ENERGY
KW  - RECOGNITION
KW  - SPECIFICITY
UR  - http://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0189375&type=printable
L2  - http://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0189375&type=printable
N2  - Protein-carbohydrate interactions are very often mediated by the stacking CH-pi interactions involving the side chains of aromatic amino acids such as tryptophan (Trp), tyrosine (Tyr) or phenylalanine (Phe). Especially suitable for stacking is the Trp residue. Analysis of the PDB database shows Trp stacking for 265 carbohydrate or carbohydrate-like ligands in 5 208 Trp-containing motives. An appropriate model system to study such an interaction is the AAL lectin family, where the stacking interactions play a crucial role and are thought to be a driving force for carbohydrate binding. In this study we present data showing a novel finding in the stacking interaction of the AAL Trp side chain with the carbohydrate. High resolution X-ray structure of the AAL lectin from Aleuria aurantia with alpha-methyl-L-fucoside ligand shows two possible Trp side chain conformations with the same occupation in electron density. The in silico data shows that the conformation of the Trp side chain does not influence the interaction energy despite the fact that each conformation creates interactions with different carbohydrate CH groups. Moreover, the PDB data search shows that the conformations are almost equally distributed across all Trp-carbohydrate complexes, which would suggest no substantial preference for one conformation over another.
ER  -

HOUSER, Josef, Stanislav KOZMON, Deepti MISHRA, Sushil Kumar MISHRA, Patrick R ROMANO, Michaela WIMMEROVÁ and Jaroslav KOČA. Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL. \textit{Plos one}. San Francisco: Public Library of Science, 2017, vol.~12, No~12, p.~0189375-189391. ISSN~1932-6203. Available from: https://dx.doi.org/10.1371/journal.pone.0189375.

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