期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 284, 期 12, 页码 7455-7464出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M808067200
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资金
- NIGMS NIH HHS [GM069611] Funding Source: Medline
- NINDS NIH HHS [NS038310] Funding Source: Medline
PEP-19 is a small calmodulin (CaM)-binding protein that greatly increases the rates of association and dissociation of Ca2+ from the C-domain of CaM, an effect that is mediated by an acidic/IQ sequence in PEP-19. We show here using NMR that PEP-19 is an intrinsically disordered protein, but with residual structure localized to its acidic/IQ motif. We also show that the k(on) and k(off) rates for binding PEP-19 to apo-CaM are at least 50-fold slower than for binding to Ca2+-CaM. These data indicate that intrinsic disorder confers plasticity that allows PEP-19 to bind to either apo- or Ca2+-CaM via different structural modes, and that complex formation may be facilitated by conformational selection of residual structure in the acidic/IQ sequence.
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