Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å

The principal elements of the secondary, tertiary and quaternary structure of the tetrameric human plasma prealbumin molecule have been determined by Fourier refinement of X-ray diffraction data at 1.8 Å resolution. The subunit has an extensive β-structure composed of eight strands organised into tw...

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Veröffentlicht in:Journal of molecular biology 1978-05, Vol.121 (3), p.339-356
Hauptverfasser: Blake, C.C.F., Geisow, M.J., Oatley, S.J., Rérat, B., Rérat, C.
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container_end_page 356
container_issue 3
container_start_page 339
container_title Journal of molecular biology
container_volume 121
creator Blake, C.C.F.
Geisow, M.J.
Oatley, S.J.
Rérat, B.
Rérat, C.
description The principal elements of the secondary, tertiary and quaternary structure of the tetrameric human plasma prealbumin molecule have been determined by Fourier refinement of X-ray diffraction data at 1.8 Å resolution. The subunit has an extensive β-structure composed of eight strands organised into two four-stranded sheets. There is also one short α-helix. The tertiary structure is largely determined by the association of the two β-sheets. Important contributions to the tertiary structure are made by three tyrosines and one aspartic acid involved in side-chain-main-chain interactions; a buried histidine associated with a group of internal water molecules; and a compact cluster of seven aromatic residues. Quaternary interactions occur at two sets of interfaces closely organised around two of the three molecular 2-fold axes. The exclusive monomer-monomer interface is chiefly concerned with antiparallel hydrogen bond interactions which extend the two four-stranded sheets in the monomers to eight-stranded sheets in the dimer. One of the sheet interactions includes water molecules and tyrosine hydroxyls in the hydrogen bond pattern. The dimers associate through both hydrophilic and hydrophobic interactions at interfaces that involve all four monomers.
doi_str_mv 10.1016/0022-2836(78)90368-6
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source MEDLINE; Access via ScienceDirect (Elsevier)
subjects Amino Acid Sequence
Hydrogen Bonding
Macromolecular Substances
Models, Molecular
Prealbumin
Protein Conformation
Serum Albumin
X-Ray Diffraction
title Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å
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