1F2R
NMR STRUCTURE OF THE HETERODIMERIC COMPLEX BETWEEN CAD DOMAINS OF CAD AND ICAD
Summary for 1F2R
| Entry DOI | 10.2210/pdb1f2r/pdb |
| Related | 1C9F |
| Descriptor | CASPASE-ACTIVATED DNASE, INHIBITOR OF CASPASE-ACTIVATED DNASE (2 entities in total) |
| Functional Keywords | alpha-beta roll, protein-protein complex, dna binding protein |
| Biological source | Mus musculus (house mouse) More |
| Cellular location | Cytoplasm: O54788 Cytoplasm (By similarity): O54786 |
| Total number of polymer chains | 2 |
| Total formula weight | 20689.62 |
| Authors | Otomo, T.,Sakahira, H.,Uegaki, K.,Nagata, S.,Yamazaki, T. (deposition date: 2000-05-29, release date: 2000-06-08, Last modification date: 2024-05-22) |
| Primary citation | Otomo, T.,Sakahira, H.,Uegaki, K.,Nagata, S.,Yamazaki, T. Structure of the heterodimeric complex between CAD domains of CAD and ICAD. Nat.Struct.Biol., 7:658-662, 2000 Cited by PubMed Abstract: We present here the structure of the complex between the CAD domain of caspase activated deoxyribonuclease (CAD) and the CAD domain of its inhibitor (ICAD), determined by nuclear magnetic resonance spectroscopy. The two domains adopt a very similar fold, which consists of an alpha-helix and a beta-sheet, and are aligned side by side in the complex. Notably, the positive charges on the strand beta2 at one end of the beta-sheet of CAD and negative charges around the opposite end of the beta-sheet of ICAD are paired in the complex. Point mutations of the charged amino acids at this interface, on either CAD or ICAD, prevented formation of the functional CAD-ICAD complex. This implies that the interaction between the CAD domains of CAD and ICAD is an essential step in the correct folding of CAD in the complex. PubMed: 10932250DOI: 10.1038/77957 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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