6W5B
N124D Deamidation Mutant of Human gammaD-Crystallin
Summary for 6W5B
| Entry DOI | 10.2210/pdb6w5b/pdb |
| Descriptor | Gamma-crystallin D (2 entities in total) |
| Functional Keywords | deamidation, lens, cataract, protein modification, structural protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 20635.96 |
| Authors | Whitley, M.J.,Rathi, N.,Ambarian, M.,Gronenborn, A.M. (deposition date: 2020-03-12, release date: 2021-01-20, Last modification date: 2023-10-18) |
| Primary citation | Guseman, A.J.,Whitley, M.J.,Gonzalez, J.J.,Rathi, N.,Ambarian, M.,Gronenborn, A.M. Assessing the Structures and Interactions of gamma D-Crystallin Deamidation Variants. Structure, 29:284-291.e3, 2021 Cited by PubMed Abstract: Cataracts involve the deposition of the crystallin proteins in the vertebrate eye lens, causing opacification and blindness. They are associated with either genetic mutation or protein damage that accumulates over the lifetime of the organism. Deamidation of Asn residues in several different crystallins has been observed and is frequently invoked as a cause of cataract. Here, we investigated the properties of Asp variants, deamidation products of γD-crystallin, by solution NMR, X-ray crystallography, and other biophysical techniques. No substantive structural or stability changes were noted for all seven Asn to Asp γD-crystallins. Importantly, no changes in diffusion interaction behavior could be detected. Our combined experimental results demonstrate that introduction of single Asp residues on the surface of γD-crystallin by deamidation is unlikely to be the driver of cataract formation in the eye lens. PubMed: 33264606DOI: 10.1016/j.str.2020.11.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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