Sandbox Reserved 1759: Difference between revisions

Line 14:

== Structural highlights ==

The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid ~~chains~~, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>.

The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>.

.In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well

MBD is ATP-~~independent but evolves from the~~ ATP-~~dependent , The~~ MBD ~~enzymes~~ ligand binding site overlaps with the ATP binding site of its homologous enzyme, DMD.

The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.

</StructureSection>

Sandbox Reserved 1759: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 14: / Line 14: @@
 == Structural highlights ==
-The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid chains, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>.
+The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>.
 .In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well
-MBD is ATP-independent but evolves from the ATP-dependent , The MBD enzymes ligand binding site overlaps with the ATP binding site of its homologous enzyme, DMD.
+ The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.
 </StructureSection>