We have been unable to cocrystallize Kapα50 with NLS containing–peptides. Results and Discussion Domain Identification and Structure Determination The protein forms a homodimer in the crystals, and this self-association has implications for a possible autoinhibitory mechanism. The number and placement of the binding sites dictate the sequence requirements for monopartite and bipartite nuclear localization signals. These sites are formed within a long surface groove that is lined by conserved solvent-exposed residues. The structure shows that the repeating architectural pattern of the arm motifs is utilized by the protein to generate an array of binding sites that are specific for lysine and arginine. cerevisiae karyopherin α in the unliganded form and in a complex with a peptide corresponding to the NLS of the SV40 large T antigen. We now report the crystal structures of the entire arm-repeat region of S. In the absence of three-dimensional structural information, it has been difficult to explain the diversity of NLS motifs, as well as the constraints on their sequences. ScannerMaster is proud to sell ARC software products for scanners from Butel.Little is known at present regarding the molecular mechanism underlying the recognition of nuclear localization signals by karyopherin α.
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