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Article

Steroid ligands bind human sex hormone-binding globulin in specific orientations and produce distinct changes in protein conformation.

The Journal of biological chemistry - 30 Aug 2002

Grishkovskaya Irina, Avvakumov George V, Hammond Geoffrey L, Catalano Maria G, Muller Yves A

Abstract excerpt

The amino-terminal laminin G-like domain of human sex hormone-binding globulin (SHBG) contains a single high affinity steroid-binding site. Crystal structures of this domain in complex with several different steroid ligands have revealed that estradiol occupies the SHBG steroid-binding site in an opposite orientation when compared with 5 alpha-dihydrotestosterone or C19 androgen metabolites (5 alpha-androstan-3...

Read the complete abstract on PubMed

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Share to Amino Acid Substitution
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Mutagenesis, Site-Directed

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Share to Sex Hormone-Binding Globulin

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Source

Identifiers

PMID: 12065592
DOI: 10.1074/jbc.M203999200

Genes

SHBG

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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