Structure of oxidized α-haemoglobin bound to AHSP reveals a protective mechanism for haem

Liang Feng, Suiping Zhou, Lichuan Gu, David A. Gell, Joel P. Mackay, Mitchell J. Weiss, Andrew J. Gow () and Yigong Shi ()
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Liang Feng: Princeton University
Suiping Zhou: The Children's Hospital of Philadelphia and the University of Pennsylvania
Lichuan Gu: Princeton University
David A. Gell: University of Sydney
Joel P. Mackay: University of Sydney
Mitchell J. Weiss: The Children's Hospital of Philadelphia and the University of Pennsylvania
Andrew J. Gow: The Children's Hospital of Philadelphia and the University of Pennsylvania
Yigong Shi: Princeton University

Nature, 2005, vol. 435, issue 7042, 697-701

Abstract: Haem truths Free α-haemoglobin exists as a structurally unstable monomer and is prone to oxidation and precipitation, contributing to the pathophysiology of β-thalassaemia and other blood disorders. Molecular chaperones had long been proposed to help stabilize free α-haemoglobin, and several years ago one was discovered: α-haemoglobin stabilizing protein (AHSP), which specifically interacts with and stabilizes free α-haemoglobin. The crystal structure of AHSP bound to the oxidized Fe(III) α-haemoglobin has now been determined, revealing how the haem group is protected via a mechanism that requires α-haemoglobin to undergo drastic structural rearrangements.

Date: 2005
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DOI: 10.1038/nature03609

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