5M9J
Human angiogenin PD variant K60E
Summary for 5M9J
Entry DOI | 10.2210/pdb5m9j/pdb |
Descriptor | Angiogenin, L(+)-TARTARIC ACID (3 entities in total) |
Functional Keywords | parkinson's, rnase, angiogenesis, hydrolase |
Biological source | Homo sapiens (Human) |
Cellular location | Cytoplasmic vesicle, secretory vesicle lumen : P03950 |
Total number of polymer chains | 1 |
Total formula weight | 14450.25 |
Authors | Bradshaw, W.J.,Rehman, S.,Pham, T.T.K.,Thiyagarajan, N.,Lee, R.L.,Subramanian, V.,Acharya, K.R. (deposition date: 2016-11-01, release date: 2017-02-22, Last modification date: 2024-11-13) |
Primary citation | Bradshaw, W.J.,Rehman, S.,Pham, T.T.,Thiyagarajan, N.,Lee, R.L.,Subramanian, V.,Acharya, K.R. Structural insights into human angiogenin variants implicated in Parkinson's disease and Amyotrophic Lateral Sclerosis. Sci Rep, 7:41996-41996, 2017 Cited by PubMed Abstract: Mutations in Angiogenin (ANG), a member of the Ribonuclease A superfamily (also known as RNase 5) are known to be associated with Amyotrophic Lateral Sclerosis (ALS, motor neurone disease) (sporadic and familial) and Parkinson's Disease (PD). In our previous studies we have shown that ANG is expressed in neurons during neuro-ectodermal differentiation, and that it has both neurotrophic and neuroprotective functions. In addition, in an extensive study on selective ANG-ALS variants we correlated the structural changes to the effects on neuronal survival and the ability to induce stress granules in neuronal cell lines. Furthermore, we have established that ANG-ALS variants which affect the structure of the catalytic site and either decrease or increase the RNase activity affect neuronal survival. Neuronal cell lines expressing the ANG-ALS variants also lack the ability to form stress granules. Here, we report a detailed experimental structural study on eleven new ANG-PD/ALS variants which will have implications in understanding the molecular basis underlying their role in PD and ALS. PubMed: 28176817DOI: 10.1038/srep41996 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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