The Mad2 spindle checkpoint protein has two distinct natively folded states

By Xuelian Luo, Zhanyun Tang, Guohong Xia, Katja Wassmann, Tomohiro Matsumoto, J. Rizo, Hongtao Yu. 2004

329 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Oncology

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Citations in the corpus

Predicting multiple conformations via sequence clustering and AlphaFold2 (2023, neutral): “MAD2 has two topologically distinct monomeric structures that are in equilibrium under physiological conditions 27 .”
Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes (2006, unknown): “2).”
Prediction of multiple conformational states by combining sequence clustering with AlphaFold2 (2022, background): “Mad2 has two topologically distinct monomeric structures that are in equilibrium under physiological conditions 15 .”
Protein Metamorphosis: The Two-State Behavior of Mad2 (2008, methodology): “At the physiological temperature (37°C), O-Mad2 spontaneously converts to C-Mad2 with slow kinetics (t1/2 = 9 hrs) (Luo et al., 2004), indicating that O-Mad2 is the high-energy state and that a large energy barrier separates the two states.”
An α-helix to β-barrel domain switch transforms the transcription factor RfaH into a translationfactor (2012, unknown): “The mitotic arrest deficiency 2 protein (Mad2) also exists in two conformations that are 70% identical; C-terminal andN-terminal regions form an additional b hairpin as a key interaction partner binding site in a closed state, stabilizing it compared to the open, noninteracting form (Luo et al., 200”
Interconversion between two unrelated protein folds in the lymphotactin native state (2008, background): “Likewise, slow interconversion of a monomeric mutant of the spindle checkpoint protein Mad2 repositions a C-terminal -hairpin on an invariant core structure to allow Cdc20 binding, and at equilibrium 10% of the protein can be detected in the inactive state by NMR (4).”