Selective interactions of Co2+-Ca2+-concanavalin A with high mannose N-glycans

Yunha Hwang; Jae Hee Jeong; Dong Heon Lee; Seung Jae Lee

doi:10.1039/d3dt03575a

Selective interactions of Co²⁺-Ca²⁺-concanavalin A with high mannose N-glycans

Yunha Hwang
, Jae Hee Jeong
, Dong Heon Lee
, Seung Jae Lee^*

^*Corresponding author for this work

Department of Chemistry

Jeonbuk National University
Pohang University of Science and Technology

Research output: Contribution to journal › Journal article › peer-review

2 Scopus citations

Abstract

Concanavalin A (ConA) has an intrinsic binding affinity to carbohydrates. Here, we obtained Co²⁺-Ca²⁺-ConA (2.83 Å, PDB: 8I7Q) via X-ray crystallography by substituting native ConA (Mn²⁺-Ca²⁺); it has binding selectivity for high-mannose N-glycan similar to native ConA. Our findings may thus inform antiviral reagent design.

Original language	English
Pages (from-to)	428-433
Number of pages	6
Journal	Dalton Transactions
Volume	53
Issue number	2
DOIs	https://doi.org/10.1039/d3dt03575a
State	Published - 2023.12.5

Quacquarelli Symonds(QS) Subject Topics

Chemistry

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title = "Selective interactions of Co2+-Ca2+-concanavalin A with high mannose N-glycans",

abstract = "Concanavalin A (ConA) has an intrinsic binding affinity to carbohydrates. Here, we obtained Co2+-Ca2+-ConA (2.83 {\AA}, PDB: 8I7Q) via X-ray crystallography by substituting native ConA (Mn2+-Ca2+); it has binding selectivity for high-mannose N-glycan similar to native ConA. Our findings may thus inform antiviral reagent design.",

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T1 - Selective interactions of Co2+-Ca2+-concanavalin A with high mannose N-glycans

AU - Hwang, Yunha

AU - Jeong, Jae Hee

AU - Lee, Dong Heon

AU - Lee, Seung Jae

PY - 2023/12/5

Y1 - 2023/12/5

N2 - Concanavalin A (ConA) has an intrinsic binding affinity to carbohydrates. Here, we obtained Co2+-Ca2+-ConA (2.83 Å, PDB: 8I7Q) via X-ray crystallography by substituting native ConA (Mn2+-Ca2+); it has binding selectivity for high-mannose N-glycan similar to native ConA. Our findings may thus inform antiviral reagent design.

AB - Concanavalin A (ConA) has an intrinsic binding affinity to carbohydrates. Here, we obtained Co2+-Ca2+-ConA (2.83 Å, PDB: 8I7Q) via X-ray crystallography by substituting native ConA (Mn2+-Ca2+); it has binding selectivity for high-mannose N-glycan similar to native ConA. Our findings may thus inform antiviral reagent design.

UR - https://www.scopus.com/pages/publications/85179790181

U2 - 10.1039/d3dt03575a

DO - 10.1039/d3dt03575a

M3 - Journal article

C2 - 38086668

AN - SCOPUS:85179790181

SN - 1477-9226

VL - 53

SP - 428

EP - 433

JO - Dalton Transactions

JF - Dalton Transactions

IS - 2

ER -

Selective interactions of Co²⁺-Ca²⁺-concanavalin A with high mannose N-glycans

Abstract

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