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      Crystal structure of human serum albumin at 2.5 Å resolution

      , , , ,
      Protein Engineering, Design and Selection
      Oxford University Press (OUP)

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          Most cited references17

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          The Protein Data Bank. A computer-based archival file for macromolecular structures.

          The Protein Data Bank is a computer-based archival file for macromolecular structures. The Bank stores in a uniform format atomic co-ordinates and partial bond connectivities, as derived from crystallographic studies. Text included in each data entry gives pertinent information for the structure at hand (e.g. species from which the molecule has been obtained, resolution of diffraction data, literature citations and specifications of secondary structure). In addition to atomic co-ordinates and connectivities, the Protein Data Bank stores structure factors and phases, although these latter data are not placed in any uniform format. Input of data to the Bank and general maintenance functions are carried out at Brookhaven National Laboratory. All data stored in the Bank are available on magnetic tape for public distribution, from Brookhaven (to laboratories in the Americas), Tokyo (Japan), and Cambridge (Europe and worldwide). A master file is maintained at Brookhaven and duplicate copies are stored in Cambridge and Tokyo. In the future, it is hoped to expand the scope of the Protein Data Bank to make available co-ordinates for standard structural types (e.g. alpha-helix, RNA double-stranded helix) and representative computer programs of utility in the study and interpretation of macromolecular structures.
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            Atomic structure and chemistry of human serum albumin.

            The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 A. It comprises three homologous domains that assemble to form a heart-shaped molecule. Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. The structure explains numerous physical phenomena and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serum albumin.
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              Accurate bond and angle parameters for X-ray protein structure refinement

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                Author and article information

                Journal
                Protein Engineering, Design and Selection
                Oxford University Press (OUP)
                1741-0134
                1741-0126
                June 1999
                June 01 1999
                June 1999
                June 1999
                June 01 1999
                June 1999
                : 12
                : 6
                : 439-446
                Article
                10.1093/protein/12.6.439
                10388840
                10bed694-e88e-41c0-9eeb-0e5c054b6127
                © 1999
                History

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