3bsqA Discussion: Difference between revisions
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'''Multiple sequence alighment''' (MSA) revealed some conserved residues throughput the whole sulfatase family. Previous experiemnts describe a set of crutial residues for the sulfatase function of an enzyme. A histidine residue (H) and two or more sequential arganine residues (R) are known to be essential, and also characteristic of the N-terminal active site of sulfatases. Our MSA resultaes | '''Multiple sequence alighment''' (MSA) revealed some conserved residues throughput the whole sulfatase family. Previous experiemnts describe a set of crutial residues for the sulfatase function of an enzyme. A histidine residue (H) and two or more sequential arganine residues (R) are known to be essential, and also characteristic of the N-terminal active site of sulfatases. Our MSA resultaes a set of residues conserves in the N-terminus, along with a H and one R residue. When these conserved residues were marked in the three dimenetional view of ASK in PyMol, they all seemed clustered within a certain region of the molecule. moreover, this region is deep inside the molecule, directly inside a pocket-like surface feature. This region is assumed to be the 'possible active site' of the protein. | ||
Results of structural comparisons | Results of structural comparisons and protein-protein interactions resulted several other proteins, which were used for a second multiple sequence alighment. This alighment also showed a certain degree of conservation of previously described conserved residues. | ||
Revision as of 04:01, 2 June 2008
Multiple sequence alighment (MSA) revealed some conserved residues throughput the whole sulfatase family. Previous experiemnts describe a set of crutial residues for the sulfatase function of an enzyme. A histidine residue (H) and two or more sequential arganine residues (R) are known to be essential, and also characteristic of the N-terminal active site of sulfatases. Our MSA resultaes a set of residues conserves in the N-terminus, along with a H and one R residue. When these conserved residues were marked in the three dimenetional view of ASK in PyMol, they all seemed clustered within a certain region of the molecule. moreover, this region is deep inside the molecule, directly inside a pocket-like surface feature. This region is assumed to be the 'possible active site' of the protein.
Results of structural comparisons and protein-protein interactions resulted several other proteins, which were used for a second multiple sequence alighment. This alighment also showed a certain degree of conservation of previously described conserved residues.
