2gnx Abstract: Difference between revisions
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The evolutionary analysis aimed to show the divergence of this protein in a verity of species. It was found that this protein is mainly present in higher metazoans and that insects and sea urchins diverged greatest from the target protein of interest. The presence of this protein only in higher metazoans indicates it is not a crucial survival, and developed later in evolution. | |||
Structural analysis of the hypothetical 2GNX protein was not able to identify any structurally similar proteins for the N-terminal domain. A structurally similar protein was however identified for the C-terminal domain and this was the GAF protein. It was predicted that cGMP ligand, which binds to GAF protein, may also bind to a pocket in 2GNX. | Structural analysis of the hypothetical 2GNX protein was not able to identify any structurally similar proteins for the N-terminal domain. A structurally similar protein was however identified for the C-terminal domain and this was the GAF protein. It was predicted that cGMP ligand, which binds to GAF protein, may also bind to a pocket in 2GNX. | ||
By carrying out functional analysis, it was hypothesized that the hypothetical protein 2GNX is involved in the olfactory transduction pathway. Olfactory mechanisms are a significant part of the genome as the receptors constitute the largest gene superfamily in the vertebrate genome. There are over 900 olfactory receptor genes present in the human genome. Thus this protein could present significant knowledge with further research. | |||
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Latest revision as of 01:50, 12 June 2007
The evolutionary analysis aimed to show the divergence of this protein in a verity of species. It was found that this protein is mainly present in higher metazoans and that insects and sea urchins diverged greatest from the target protein of interest. The presence of this protein only in higher metazoans indicates it is not a crucial survival, and developed later in evolution.
Structural analysis of the hypothetical 2GNX protein was not able to identify any structurally similar proteins for the N-terminal domain. A structurally similar protein was however identified for the C-terminal domain and this was the GAF protein. It was predicted that cGMP ligand, which binds to GAF protein, may also bind to a pocket in 2GNX.
By carrying out functional analysis, it was hypothesized that the hypothetical protein 2GNX is involved in the olfactory transduction pathway. Olfactory mechanisms are a significant part of the genome as the receptors constitute the largest gene superfamily in the vertebrate genome. There are over 900 olfactory receptor genes present in the human genome. Thus this protein could present significant knowledge with further research.
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