Calmodulin Binds a Highly Extended HIV-1 MA Protein That Refolds Upon Its Release

(Biophysical Journal 103, August 2012; 541–549) The authors identified an omission in this article. The figure legend for Figure S2 should include the following: “The model displayed here includes full-length calcium-bound CaM and the matrix protein sequence spanning amino acids 1–113; i.e., it does not include the flexible C-terminal tail (amino acids 114–133).” None of the article’s conclusions are affected by this omission. In addition, after publication of the article, the SAXS and SANS data and modeling for this article were deposited in the Small Angle Scattering Biological Data Bank (SASBDB; https://www.sasbdb.org/) under accession code SASDKR3. Finally, the first author’s name should appear as “James E. N. Taylor” rather than “James E. Taylor.” Calmodulin Binds a Highly Extended HIV-1 MA Protein That Refolds Upon Its ReleaseTaylor et al.Biophysical JournalAugust 08, 2012In BriefCalmodulin (CaM) expression is upregulated upon HIV-1 infection and interacts with proteins involved in viral processing, including the multifunctional HIV-1 MA protein. We present here the results of studies utilizing small-angle neutron scattering with contrast variation that, when considered in the light of earlier fluorescence and NMR data, show CaM binds MA in an extended open-clamp conformation via interactions with two tryptophans that are widely spaced in sequence and space. The interaction requires a disruption of the MA tertiary fold such that MA becomes highly extended in a long snakelike conformation. Full-Text PDF Open Archive