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Article

The minimal α-crystallin domain of Mj Hsp16.5 is functional at non-heat-shock conditions.

Proteins - 1 Jul 2014

Xi Dong, Wei Ping, Zhang Changsheng, Lai Luhua

Abstract excerpt

The small heat shock protein (sHSP) from Methanococcus jannaschii (Mj Hsp16.5) forms a monodisperse 24mer and each of its monomer contains two flexible N- and C-terminals and a rigid α-crystallin domain with an extruding β-strand exchange loop. The minimal α-crystallin domain with a β-sandwich fold is conserved in sHSP family, while the presence of the β-strand exchange loop is divergent. The function of the...

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PMID: 24243469
DOI: 10.1002/prot.24480

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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