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Article

Structure of fully liganded Hb ζ2β2s trapped in a tense conformation.

Acta crystallographica. Section D, Biological crystallography - 1 Oct 2013

Safo Martin K, Ko Tzu-Ping, Abdulmalik Osheiza, He Zhenning, Wang Andrew H-J, Schreiter Eric R, Russell J Eric

Abstract excerpt

A variant Hb ζ2β2(s) that is formed from sickle hemoglobin (Hb S; α2β2(s)) by exchanging adult α-globin with embryonic ζ-globin subunits shows promise as a therapeutic agent for sickle-cell disease (SCD). Hb ζ2β2(s) inhibits the polymerization of deoxygenated Hb S in vitro and reverses characteristic features of SCD in vivo in mouse models of the disorder. When compared with either Hb S or with normal human adult...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 24100324
DOI: 10.1107/S0907444913019197
PMCID: PMC3792644

Genes

SCD

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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