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Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex
Authors
Brubaker, K., Cowley, S.M., Huang, K., Eisenman, R.N., Radhakrishnan, I.
Assembly
MAD1 PROTEIN/SIN3A
Entity
1. MAD1 SID domain (polymer, Thiol state: not present), 16 monomers, 1966.285 Da Detail

RMNIQMLLEA ADYLER


2. mSin3A PAH2 Domain (polymer, Thiol state: not present), 89 monomers, 10332.35 Da Detail

SLQNNQPVEF NHAINYVNKI KNRFQGQPDI YKAFLEILHT YQKEQRNAKE AGGNYTPALT EQEVYAQVAR LFKNQEDLLS EFGQFLPDA


Total weight
12298.635 Da
Max. entity weight
10332.35 Da
Exptl. method
NMR
Refine. method
distance geometry, simulated annealing
Data set
coupling_constants
Protein Blocks Logo
Calculated from 15 models in PDB: 1G1E, Strand ID: A, B Detail


Coupling constant
72 J values in 1 lists
Field strength (1H) 500 MHz, Pressure 1 atm, Temperature 300 K, pH 6.0 Detail
Release date
2001-05-06
Citation
Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex
Brubaker, K., Cowley, S.M., Huang, K., Loo, L., Yochum, G.S., Ayer, D.E., Eisenman, R.N., Radhakrishnan, I.
Cell (2000), 103, 655-665, PubMed 11106735 , DOI: ,
Related entities 1. MAD1 SID domain, : 1 : 4 : 1 : 9 entities Detail
Related entities 2. mSin3A PAH2 Domain, : 5 : 126 entities Detail
Interaction partners 1. MAD1 SID domain, : 6 : 1 interactors Detail
Interaction partners 2. mSin3A PAH2 Domain, : 33 interactors Detail
Experiments performed 7 experiments Detail
nullKeywords Four-helix bundle, Protein-peptide Complex