DHRS1 Discussion: Difference between revisions
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==Structure== | ==Structure== | ||
HA! first | HA! first | ||
Although the SDR family show low sequence identity (15-20%) they have highly conserved structural features in particular the NAD(P) binding site, central β-strand and co-enzyme binding site. | |||
DHRS1 has been crystallized to a resolution of 1.8 Å with an R-value of 0.159. This R-value however was achieved without recording a highly mobile region of 22 amino acids which covers over the NAD(P) binding site, and may act as a cap locking the NAD(P) into the binding site. | |||
Structural alignments with other members of the SDR family showed that the most closely structurally related proteins where all involved in reducing substrates (reductases). In particular Glucose reductases appeared frequently (Table 1). | |||
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[[Dehydrogenase/reductase (SDR family) member 1 | Back to Main Page]] | [[Dehydrogenase/reductase (SDR family) member 1 | Back to Main Page]] | ||
Revision as of 07:54, 3 June 2008
Structure
HA! first
Although the SDR family show low sequence identity (15-20%) they have highly conserved structural features in particular the NAD(P) binding site, central β-strand and co-enzyme binding site.
DHRS1 has been crystallized to a resolution of 1.8 Å with an R-value of 0.159. This R-value however was achieved without recording a highly mobile region of 22 amino acids which covers over the NAD(P) binding site, and may act as a cap locking the NAD(P) into the binding site.
Structural alignments with other members of the SDR family showed that the most closely structurally related proteins where all involved in reducing substrates (reductases). In particular Glucose reductases appeared frequently (Table 1).
