Highly conserved residues among ligand binding domains of steroid receptors

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  • ステロイド受容体リガンド結合ドメインにおいて高度に保存されているアミノ酸残基

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To clarify a meaning of "conserved residues", ligand-binding domains of steroid receptors are used as a model data set for sequence-function relationships. In this study, ligand-binding, dimerization, and HSP90-binding were mainly forcused. Multiple sequence alignment of 39 ligand-binding domains of steroid receptors was performed introducing information about their 3D-structures. As the result of the alignment, 36 residues were conserved in more than 80% of the sequences. They were distributed on all over the sequence, however, on the 3D-structure, they were located closely each other and making a core of the domain. Only a few residues could be observed on the surface. To pick up candidates for dimerization, I propose an application method using the difference of accessible surface areas between dimer and monomer calculated by the DSSP program. The results comparing the residues and biochemical function sites indicate that the highly conserved residues are corresponding to ligand-binding directly, however, not related to dimerization and HSP90-binding. It suggests that the highly conserved residues form a certain 3D-structure and switch to another structure concerning with co-factor binding or releasing.

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