NMR chemical shift assignments for androcam, a testis-specific myosin VI light chain in D. melanogaster.
Androcam is a D. melanogaster calmodulin-like protein expressed exclusively in the testis that interacts with myosin VI and is critical to spermatogenesis. At micromolar free Ca(2+), androcam binds two calcium ions using its C-terminal lobe but its N-terminal lobe is Ca(2+)-free. We are pursuing structural studies on androcam at physiological (10 μM) and high (10 mM) calcium. Here we report the (1)H, (15)N, and (13)C chemical shifts of androcam at 10 μM free Ca(2+) determined using multi-dimensional NMR experiments.
Department of Biochemistry and Cell Biology, Rice University, Houston, TX 77254, USA.
Mehul K
MK
Joshi
Sean
S
Moran
Kevin R
KR
MacKenzie
D000595:Amino Acid Sequence; D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D029721:Drosophila Proteins / Q000737:chemistry*; D004331:Drosophila melanogaster / Q000378:metabolism*; D008297:Male; D018995:Myosin Heavy Chains / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D009928:Organ Specificity; D013737:Testis / Q000378:metabolism*
C090181:Acam protein, Drosophila; D002135:Calcium-Binding Proteins; D029721:Drosophila Proteins; C089785:myosin VI; D018995:Myosin Heavy Chains