Sandbox Reserved 1101: Difference between revisions
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Different types of interactions occur between specific residues during the NTD dimerization. Asp40, Lys65, Asp39 and Glu84 residues have been identified as being particularly important. | Different types of interactions occur between specific residues during the NTD dimerization. Asp40, Lys65, Asp39 and Glu84 residues have been identified as being particularly important. | ||
In one side, Asp40 and Glu84 of subunit A engage in the intramolecular handshake interaction. <scene name='82/829354/Lys_65-asp39_interaction/1'>Lys65 of subunit A and Asp39 of subunit B</scene> engage in a short-range intermolecular salt bridge of 2,6Å. In the other side, Asp40 of subunit A and Lys65 of subunit B engage in a short-range intermolecular salt bridge of 3,1Å. Asp39 is not involved in this part of the dimer. | In one side, Asp40 and Glu84 of subunit A engage in the intramolecular handshake interaction. <scene name='82/829354/Lys_65-asp39_interaction/1'>Lys65 of subunit A and Asp39 of subunit B</scene> engage in a short-range intermolecular salt bridge of 2,6Å. In the other side, <scene name='82/829354/Lys_65b-asp40a_interaction/1'>Asp40 of subunit A and Lys65 of subunit B</scene> engage in a short-range intermolecular salt bridge of 3,1Å. Asp39 is not involved in this part of the dimer. | ||
The structure of ''N. clavipes'' dimer interface differs from those of other species due to the asymmetric nature of the interface and the involvement of Asp39. It has been reported that Asp39 is essential for the NTD dimerization in other species of spiders (16). The asymmetric nature and the difference of topology of the subunits allow the formation of salt bridges between Asp39 and Lys65 and between Asp40 and Lys65. These interactions make subunits alignment better. Acidic residues are conserved around residues Asp96 and Asp40 and this allows the variability in the interactions that take place to Lys65. This variability provides a mechanism for plasticity in the dimer interface allowing the transition from loosely to stably associated dimer. | The structure of ''N. clavipes'' dimer interface differs from those of other species due to the asymmetric nature of the interface and the involvement of Asp39. It has been reported that Asp39 is essential for the NTD dimerization in other species of spiders (16). The asymmetric nature and the difference of topology of the subunits allow the formation of salt bridges between Asp39 and Lys65 and between Asp40 and Lys65. These interactions make subunits alignment better. Acidic residues are conserved around residues Asp96 and Asp40 and this allows the variability in the interactions that take place to Lys65. This variability provides a mechanism for plasticity in the dimer interface allowing the transition from loosely to stably associated dimer. | ||
