The crystal structure of the β subunit of luteinizing hormone and a model for the intact hormone.
Crystallography
Glycosylation
Gonadotropic hormone
Pituitary hormone
Proteolysis
Reproduction
Journal
Current research in structural biology
ISSN: 2665-928X
Titre abrégé: Curr Res Struct Biol
Pays: Netherlands
ID NLM: 101767537
Informations de publication
Date de publication:
Nov 2019
Nov 2019
Historique:
received:
22
05
2019
revised:
22
07
2019
accepted:
31
07
2019
entrez:
8
7
2021
pubmed:
12
8
2019
medline:
12
8
2019
Statut:
epublish
Résumé
The β subunit of bovine luteinizing hormone (LH) was crystallized and its structure solved to 3.15 Å resolution by molecular replacement using human chorionic gonadotropin (hCG) β subunit as search model. The asymmetric unit contains two copies of the β subunit that are related by a non-crystallographic symmetry (NCS) two-fold axis, both copies of which contain proteolytic cleavages after amino acid 100. It is noteworthy that the oligosaccharide moieties covalently attached at asparagine 13 were particularly pronounced in the electron density, allowing seven sugar residues to be defined. The α subunit of LH, which is common to all glycosylated gonadotropin hormones, was placed by superposition of hCG on the LH beta subunits, thereby yielding a model for the intact hormone.
Identifiants
pubmed: 34235462
doi: 10.1016/j.crstbi.2019.07.001
pii: S2665-928X(19)30001-7
pmc: PMC8244496
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1-5Informations de copyright
© 2019 The Authors.
Références
Mol Cell Endocrinol. 2014 Jan 25;382(1):424-451
pubmed: 24001578
Structure. 1994 Jun 15;2(6):545-58
pubmed: 7922031
Cell. 1993 May 7;73(3):421-4
pubmed: 8490958
Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55
pubmed: 15299926
J Biol Chem. 2004 Aug 20;279(34):35449-57
pubmed: 15161904
J Mol Biol. 1999 Jun 25;289(5):1375-85
pubmed: 10373373
Biochem Biophys Res Commun. 1975 Nov 3;67(1):149-55
pubmed: 1201015
J Biol Chem. 1976 Oct 25;251(20):6388-91
pubmed: 988020
Nature. 1984 Jan 5-11;307(5946):37-40
pubmed: 6690982
Int J Pept Protein Res. 1981 Jul;18(1):79-87
pubmed: 7309370
Acta Crystallogr D Biol Crystallogr. 1999 Oct;55(Pt 10):1718-25
pubmed: 10531521
Mol Cell Endocrinol. 2007 Jan 2;260-262:73-82
pubmed: 17045735
Nature. 2005 Jan 20;433(7023):269-77
pubmed: 15662415
Nature. 1991 Dec 5;354(6352):411-4
pubmed: 1956407
Biochim Biophys Acta. 1988 Jun 9;947(2):287-306
pubmed: 3130893
Mol Endocrinol. 2001 Mar;15(3):378-89
pubmed: 11222739
Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):458-64
pubmed: 15805601
Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3
pubmed: 15299374
Int J Pept Protein Res. 1986 Jan;27(1):70-8
pubmed: 3512464
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):355-67
pubmed: 21460454
Acta Crystallogr D Biol Crystallogr. 2001 Oct;57(Pt 10):1373-82
pubmed: 11567148
J Mol Biol. 1977 May 25;112(3):535-42
pubmed: 875032
Annu Rev Biochem. 1981;50:465-95
pubmed: 6267989
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
pubmed: 15572765
Nature. 1994 Jun 9;369(6480):455-61
pubmed: 8202136
J Biol Chem. 1983 Jan 10;258(1):240-4
pubmed: 6848498
Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1124-30
pubmed: 12832754
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
pubmed: 19461840
J Mol Biol. 1968 Apr 28;33(2):491-7
pubmed: 5700707