Sandbox 154: Difference between revisions

Each F-actin monomeric unit has, as part of its tertiary structure, several loops that are important to its assembly to the polymeric F-actin. These loops undergo conformational changes based on the state of the bound nucleotide or they serve as regions for adjacent monomeric actin units to bind to. The <scene name='Sandbox_154/2zwh_regions_hic73/1'>sensor loop</scene> acts as a "switch" for conformations, based on the bound nucleotide<ref name"oztug">PMID:19900461</ref>. The DNAse I-binding loop <scene name='Sandbox_154/2zwh_regions_dloop/1'>(D-loop)</scene> residues (40-50) in addition to undergoing conformational changes that impact stability bind DNAse I enzymes and are speculated to keep a hold on the DNAse I<ref name="Graceffa">PMID:12813032</ref>. The hydrophobic loop <scene name='Sandbox_154/2zwh_regions_hloop/1'>(H-loop)</scene> , spanning residues 264-273, and the <scene name='Sandbox_154/2zwh_regions_wloop/1'>W-loop</scene>, spanning residues 165-172, function as sites to which adjacent actin monomer D-loops may bind to<ref name="oztug">PMID:19900461</ref>. A similar function is noted for the <scene name='Sandbox_154/2wzh_regions_cterm/2'>C-terminus</scene> residues (374-375).