6N5C
Crystal structure of the catalytic domain of PPIP5K2 in complex with AMPPNP and 5-PCF2Am-InsP5
Summary for 6N5C
| Entry DOI | 10.2210/pdb6n5c/pdb |
| Descriptor | Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (7 entities in total) |
| Functional Keywords | inositol, inositol polyphosphate, inositol pyrophosphate, analog, phosphonodifluoroacetamide, diphosphoinositol pentakisphosphate, kinase, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 39396.85 |
| Authors | Wang, H.,Shears, S.B.,Riley, A.,Potter, B. (deposition date: 2018-11-21, release date: 2019-08-21, Last modification date: 2023-10-11) |
| Primary citation | Riley, A.M.,Wang, H.,Shears, S.B.,Potter, B.V.L. Synthesis of an alpha-phosphono-alpha , alpha-difluoroacetamide analogue of the diphosphoinositol pentakisphosphate 5-InsP7. Medchemcomm, 10:1165-1172, 2019 Cited by PubMed Abstract: Diphosphoinositol phosphates (PP-InsPs) are an evolutionarily ancient group of signalling molecules that are essential to cellular and organismal homeostasis. As the detailed mechanisms of PP-InsP signalling begin to emerge, synthetic analogues of PP-InsPs containing stabilised mimics of the labile diphosphate group can provide valuable investigational tools. We synthesised 5-PCFAm-InsP (), a novel fluorinated phosphonate analogue of 5-PP-InsP, and obtained an X-ray crystal structure of in complex with diphosphoinositol pentakisphosphate kinase 2 (PPIP5K2). 5-PCFAm-InsP binds to the kinase domain of PPIP5K2 in a similar orientation to that of the natural substrate 5-PP-InsP and the PCFAm structure can mimic many aspects of the diphosphate group in 5-PP-InsP. We propose that , the structural and electronic properties of which are in some ways complementary to those of existing phosphonoacetate and methylenebisphosphonate analogues of 5-PP-InsP, may be a useful addition to the expanding array of chemical tools for the investigation of signalling by PP-InsPs. The PCFAm group may also deserve attention for wider application as a diphosphate mimic. PubMed: 31391889DOI: 10.1039/c9md00163h PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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