1GD4
SOLUTION STRUCTURE OF P25S CYSTATIN A
Summary for 1GD4
| Entry DOI | 10.2210/pdb1gd4/pdb |
| Related | 1CYU 1CYV 1GD3 |
| Descriptor | CYSTATIN A (1 entity in total) |
| Functional Keywords | cystatin a, thiol protease inhibitor, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P01040 |
| Total number of polymer chains | 1 |
| Total formula weight | 10992.39 |
| Authors | Shimba, N.,Kariya, E.,Tate, S.,Kaji, H.,Kainosho, M. (deposition date: 2000-09-08, release date: 2001-09-08, Last modification date: 2023-12-27) |
| Primary citation | Shimba, N.,Kariya, E.,Tate, S.,Kaji, H.,Kainosho, M. Structural comparison between wild-type and P25S human cystatin A by NMR spectroscopy. Does this mutation affect the a-helix conformation ? J.STRUCT.FUNCT.GENOM., 1:26-42, 2000 Cited by PubMed Abstract: The effect of substituting Pro25, located in the alpha-helical region of the cystatin A structure, with Ser has been studied. The structures of wild type and P25S cystatin A were determined by multidimensional NMR spectroscopy under comparable conditions. These two structures were virtually identical, and the alpha-helix between Glu15-Lys30 exists with uninterrupted continuity, with a slight bend at residue 25. In order to characterize the possible substitution effects of Pro25 with Ser on the alpha-helix, the chemical shifts of the amide nitrogens and protons, the generalized order parameters obtained by the analyses of the 15N-1H relaxation data, the amide proton exchange rates, and the NOE networks among the alpha-helical and surrounding residues were carefully compared. None of these parameters indicated any significant static or dynamic structural differences between the alpha-helical regions of the wild-type and P25S cystatin A proteins. We therefore conclude that our previous structure of the wild-type cystatin A, in which the alpha-helix exhibited a sharp kink at Pro25, must be revised. The asymmetric distribution of hydrophobic interactions between the side-chain residues of the alpha-helix and the rolled beta-sheet surface, as revealed by NOEs, may be responsible for the slight bend of the alpha-helix in both variants and for the destabilized hydrogen bonding of the alpha-helical residues that follow Pro25/Ser25, as evidenced by increased amide exchange rates. PubMed: 12836678DOI: 10.1023/A:1011380315619 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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