The structure of α-haemoglobin in complex with a haemoglobin-binding domain fromStaphylococcus aureusreveals the elusive α-haemoglobin dimerization interface
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چکیده
منابع مشابه
AHSP (α-haemoglobin-stabilizing protein) stabilizes apo-α-haemoglobin in a partially folded state.
To produce functional Hb (haemoglobin), nascent α-globin (αo) and β-globin (βo) chains must each bind a single haem molecule (to form αh and βh) and interact together to form heterodimers. The precise sequence of binding events is unknown, and it has been suggested that additional factors might enhance the efficiency of Hb folding. AHSP (α-haemoglobin-stabilizing protein) has been shown previou...
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Haptoglobin binding to haemoglobin and its isolated a and #-chains was studied by use of a highly sensitive solid-phase radiometric assay. As expected, adsorbents of haemoglobin bound '25I-labelled haptoglobin more efficiently than did adsorbents of the (achain. However, unexpectedly, adsorbents of the f-chain were found to be essentially identical with those of the a-chain in their ability to ...
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Haemoglobin Howick shows a high oxygen affinity (p50 = 1 mmHg) and a low co-operativity (n = 1.3). Equilibrium studies show the protein to be essentially totally dimeric in the oxygenated form. A wide range of rapid kinetic experiments indicate that the deoxygenated form of the protein exists in a tetramer<-->dimer equilibrium with an associated equilibrium constant of 3 microM. These kinetic d...
متن کاملThe structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket.
Staphylococcus aureus is a common and serious cause of infection in humans. The bacterium expresses a cell-surface receptor that binds to, and strips haem from, human haemoglobin (Hb). The binding interface has previously been identified; however, the structural changes that promote haem release from haemoglobin were unknown. Here, the structure of the receptor-Hb complex is reported at 2.6 Å r...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology Communications
سال: 2014
ISSN: 2053-230X
DOI: 10.1107/s2053230x14012175