2LHA
Solution structure of C2B with IP6
Summary for 2LHA
| Entry DOI | 10.2210/pdb2lha/pdb |
| NMR Information | BMRB: 17838 |
| Descriptor | Synaptotagmin-1, INOSITOL HEXAKISPHOSPHATE (2 entities in total) |
| Functional Keywords | protein-drug complex, beta-sheet protein, calcium binding protein, metal binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 18012.24 |
| Authors | Joung, M.,Mohan, S.K.,Yu, C. (deposition date: 2011-08-08, release date: 2012-05-02, Last modification date: 2024-05-15) |
| Primary citation | Joung, M.,Mohan, S.K.,Yu, C. Molecular Level Interaction of Inositol Hexaphosphate with the C2B Domain of Human Synaptotagmin I Biochemistry, 2012 Cited by PubMed Abstract: Synaptotagmin I is a synaptic vesicle membrane protein that serves as a multifunctional regulator during the exocytosis of neurotransmitter release. It contains C2A and C2B domains. The binding of Ca(2+) to the C2A domain activates the exocytosis of secretory vesicles, while the binding of inositol polyphosphates (IP4-IP6) to the C2B domain inhibits this process. To understand the IP6-induced inhibition of exocytosis of secretory vesicles, we determined the three-dimensional structure of the C2B-IP6 complex by nuclear magnetic resonance (NMR). In this study, we have determined the binding constant by isothermal titration calorimetry. The circular dichroism measurements demonstrated that IP6 can stabilize the C2B molecule. We identified the binding site using (1)H-(15)N heteronuclear single-quantum coherence spectroscopy titration data and determined the structure of the C2B-IP6 complex using multidimensional NMR studies. This information will aid in the design of better pharmacological treatments for neurological disorders. PubMed: 22475172DOI: 10.1021/bi300005w PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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