User:Alexander Rudecki/Sandbox 1: Difference between revisions

Line 30:

[[Image:Cropped_dimer.jpg|thumb|400px|right|Figure 2. A 3D graphical representation displaying the homodimer glutaminyl cyclase from ''Drosophila melanogaster'' (PDB: 4F9U). Secondary structure is depicted by red (α-helix) and yellow (β-strand) ribbons, glycosyl groups are coloured pink, while hydrogen bonds between the two monomers are shown by dotted green lines. The active site of QC contains a chelated zinc ion represented by a gray sphere. Also bound to the active site ~~of this crystal structure~~ and depicted as blue is the inhibitor 1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea.]][[Image:DromeQCActiveSite.png|thumb|300px|left|Figure 4. A comparison between the active sites of DromeQC crystalized either with a PBD150 inhibitor (right, PDB: 4F90) or without (left, PDB: 4FWU). Protein loops surrounding the active site are denoted in dark blue, providing a scaffold for a catalytic Zn<sup>2+</sup> (gray) to be chelated by three residues (light blue).The PBD150 inhibitor (red) involve interactions with W296 (yellow), F292 (green), W176 (beige) and D271 (pink).]]

[[Image:Cropped_dimer.jpg|thumb|400px|right|Figure 2. A 3D graphical representation displaying the homodimer glutaminyl cyclase from ''Drosophila melanogaster'' (PDB: 4F9U). Secondary structure is depicted by red (α-helix) and yellow (β-strand) ribbons, glycosyl groups are coloured pink, while hydrogen bonds between the two monomers are shown by dotted green lines. The active site of DromeQC contains a chelated zinc ion represented by a gray sphere. Also bound to the active site and depicted as blue is the inhibitor 1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea.]][[Image:DromeQCActiveSite.png|thumb|300px|left|Figure 4. A comparison between the active sites of DromeQC crystalized either with a PBD150 inhibitor (right, PDB: 4F90) or without (left, PDB: 4FWU). Protein loops surrounding the active site are denoted in dark blue, providing a scaffold for a catalytic Zn<sup>2+</sup> (gray) to be chelated by three residues (light blue).The PBD150 inhibitor (red) involve interactions with W296 (yellow), F292 (green), W176 (beige) and D271 (pink).]]

===Topology and Overall Structure<ref name="main"/>===

Revision as of 23:41, 31 March 2014 view source Alexander Rudecki (talk \| contribs) 167 edits No edit summary ← Older edit		Revision as of 23:46, 31 March 2014 view source Alexander Rudecki (talk \| contribs) 167 edits No edit summary Newer edit →
Line 30:		Line 30:


	[[Image:Cropped_dimer.jpg\|thumb\|400px\|right\|Figure 2. A 3D graphical representation displaying the homodimer glutaminyl cyclase from ''Drosophila melanogaster'' (PDB: 4F9U). Secondary structure is depicted by red (α-helix) and yellow (β-strand) ribbons, glycosyl groups are coloured pink, while hydrogen bonds between the two monomers are shown by dotted green lines. The active site of QC contains a chelated zinc ion represented by a gray sphere. Also bound to the active site ~~of this crystal structure~~ and depicted as blue is the inhibitor 1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea.]][[Image:DromeQCActiveSite.png\|thumb\|300px\|left\|Figure 4. A comparison between the active sites of DromeQC crystalized either with a PBD150 inhibitor (right, PDB: 4F90) or without (left, PDB: 4FWU). Protein loops surrounding the active site are denoted in dark blue, providing a scaffold for a catalytic Zn<sup>2+</sup> (gray) to be chelated by three residues (light blue).The PBD150 inhibitor (red) involve interactions with W296 (yellow), F292 (green), W176 (beige) and D271 (pink).]]		[[Image:Cropped_dimer.jpg\|thumb\|400px\|right\|Figure 2. A 3D graphical representation displaying the homodimer glutaminyl cyclase from ''Drosophila melanogaster'' (PDB: 4F9U). Secondary structure is depicted by red (α-helix) and yellow (β-strand) ribbons, glycosyl groups are coloured pink, while hydrogen bonds between the two monomers are shown by dotted green lines. The active site of DromeQC contains a chelated zinc ion represented by a gray sphere. Also bound to the active site and depicted as blue is the inhibitor 1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea.]][[Image:DromeQCActiveSite.png\|thumb\|300px\|left\|Figure 4. A comparison between the active sites of DromeQC crystalized either with a PBD150 inhibitor (right, PDB: 4F90) or without (left, PDB: 4FWU). Protein loops surrounding the active site are denoted in dark blue, providing a scaffold for a catalytic Zn<sup>2+</sup> (gray) to be chelated by three residues (light blue).The PBD150 inhibitor (red) involve interactions with W296 (yellow), F292 (green), W176 (beige) and D271 (pink).]]
	===Topology and Overall Structure<ref name="main"/>===		===Topology and Overall Structure<ref name="main"/>===