LG/LNS domains

Multiple functions - One business end?

Gabrielle Rudenko, Erhard Hohenester, Yves A. Muller

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

The three-dimensional structures of LG/LNS domains from neurexin, the laminin α2 chain and sex hormone-binding globulin reveal a close structural relationship to the carbohydrate-binding pentraxins and other lectins. However, these LG/LNS domains appear to have a preferential ligand-interaction site distinct from the carbohydrate-binding sites found in lectins, and this interaction site accommodates not only sugars but also steroids and proteins. In fact, the LG/LNS domain interaction site has features reminiscent of the antigen-combining sites in immunoglobulins. The LG/LNS domain presents an interesting case in which the fold has remained conserved but the functional sites have evolved; consequently, making predictions of structure-function relationships on the basis of the lectin fold alone is difficult.

Original languageEnglish (US)
Pages (from-to)363-368
Number of pages6
JournalTrends in Biochemical Sciences
Volume26
Issue number6
DOIs
StatePublished - Jun 1 2001
Externally publishedYes

Fingerprint

Lectins
Binding Sites
Carbohydrates
Industry
Sex Hormone-Binding Globulin
Laminin
Sugars
Immunoglobulins
Steroids
Ligands
Antigens
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

LG/LNS domains : Multiple functions - One business end? / Rudenko, Gabrielle; Hohenester, Erhard; Muller, Yves A.

In: Trends in Biochemical Sciences, Vol. 26, No. 6, 01.06.2001, p. 363-368.

Research output: Contribution to journalArticle

Rudenko, Gabrielle ; Hohenester, Erhard ; Muller, Yves A. / LG/LNS domains : Multiple functions - One business end?. In: Trends in Biochemical Sciences. 2001 ; Vol. 26, No. 6. pp. 363-368.
@article{d7fbca55db4549618363cef47d60c14a,
title = "LG/LNS domains: Multiple functions - One business end?",
abstract = "The three-dimensional structures of LG/LNS domains from neurexin, the laminin α2 chain and sex hormone-binding globulin reveal a close structural relationship to the carbohydrate-binding pentraxins and other lectins. However, these LG/LNS domains appear to have a preferential ligand-interaction site distinct from the carbohydrate-binding sites found in lectins, and this interaction site accommodates not only sugars but also steroids and proteins. In fact, the LG/LNS domain interaction site has features reminiscent of the antigen-combining sites in immunoglobulins. The LG/LNS domain presents an interesting case in which the fold has remained conserved but the functional sites have evolved; consequently, making predictions of structure-function relationships on the basis of the lectin fold alone is difficult.",
author = "Gabrielle Rudenko and Erhard Hohenester and Muller, {Yves A.}",
year = "2001",
month = "6",
day = "1",
doi = "10.1016/S0968-0004(01)01832-1",
language = "English (US)",
volume = "26",
pages = "363--368",
journal = "Trends in Biochemical Sciences",
issn = "0376-5067",
publisher = "Elsevier Limited",
number = "6",

}

TY - JOUR

T1 - LG/LNS domains

T2 - Multiple functions - One business end?

AU - Rudenko, Gabrielle

AU - Hohenester, Erhard

AU - Muller, Yves A.

PY - 2001/6/1

Y1 - 2001/6/1

N2 - The three-dimensional structures of LG/LNS domains from neurexin, the laminin α2 chain and sex hormone-binding globulin reveal a close structural relationship to the carbohydrate-binding pentraxins and other lectins. However, these LG/LNS domains appear to have a preferential ligand-interaction site distinct from the carbohydrate-binding sites found in lectins, and this interaction site accommodates not only sugars but also steroids and proteins. In fact, the LG/LNS domain interaction site has features reminiscent of the antigen-combining sites in immunoglobulins. The LG/LNS domain presents an interesting case in which the fold has remained conserved but the functional sites have evolved; consequently, making predictions of structure-function relationships on the basis of the lectin fold alone is difficult.

AB - The three-dimensional structures of LG/LNS domains from neurexin, the laminin α2 chain and sex hormone-binding globulin reveal a close structural relationship to the carbohydrate-binding pentraxins and other lectins. However, these LG/LNS domains appear to have a preferential ligand-interaction site distinct from the carbohydrate-binding sites found in lectins, and this interaction site accommodates not only sugars but also steroids and proteins. In fact, the LG/LNS domain interaction site has features reminiscent of the antigen-combining sites in immunoglobulins. The LG/LNS domain presents an interesting case in which the fold has remained conserved but the functional sites have evolved; consequently, making predictions of structure-function relationships on the basis of the lectin fold alone is difficult.

UR - http://www.scopus.com/inward/record.url?scp=0035369647&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035369647&partnerID=8YFLogxK

U2 - 10.1016/S0968-0004(01)01832-1

DO - 10.1016/S0968-0004(01)01832-1

M3 - Article

VL - 26

SP - 363

EP - 368

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

SN - 0376-5067

IS - 6

ER -