Sandbox elodie weider - Revision history

Élodie Weider at 15:37, 20 November 2009

Élodie Weider — Fri, 20 Nov 2009 15:37:27 GMT

←Older revision		Revision as of 15:37, 20 November 2009
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		+	== '''2g49 : Insulin-Degrading Enzyme''' ==
		+
		+
	== Introduction ==		== Introduction ==

Élodie Weider at 14:13, 13 November 2009

Élodie Weider — Fri, 13 Nov 2009 14:13:15 GMT

←Older revision		Revision as of 14:13, 13 November 2009
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	== Introduction ==		== Introduction ==

-	Insulin-Degrading Enzyme is a highly conserved ~~226~~ kDa ~~dimeric~~ zinc metalloprotease. It belongs to the M16A family of metalloproteases within the ME clan. It hydrolyses insulin and several amyloidogenic peptides like amyloid-β (Aβ).	+	Insulin-Degrading Enzyme is a highly conserved 2*113 kDa homodimeric zinc metalloprotease. It belongs to the M16A family of metalloproteases within the ME clan. It hydrolyses insulin and several amyloidogenic peptides like amyloid-β (Aβ).
	Aβ is the main component of brain and of the amyloid islets found in Alzheimer’s disease.		Aβ is the main component of brain and of the amyloid islets found in Alzheimer’s disease.
	Insulin is a peptide associated with diabete. The gene encoding IDE is located on human chromosome 10q and is in a region linked to type 2 diabete and Alzheimer’s disease.		Insulin is a peptide associated with diabete. The gene encoding IDE is located on human chromosome 10q and is in a region linked to type 2 diabete and Alzheimer’s disease.
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	=== Structure general points ===		=== Structure general points ===

-	IDE is a ~~dimeric~~ protein. Each IDE monomer is composed of four 25-27 kDa structurally homologous αβ roll domains:	+	IDE is a homodimeric protein. Each IDE monomer is composed of four 25-27 kDa structurally homologous αβ roll domains:
	* <scene name='Sandbox_elodie_weider/Domain_1/2'>domain 1</scene>: residues 43-285		* <scene name='Sandbox_elodie_weider/Domain_1/2'>domain 1</scene>: residues 43-285
	* <scene name='Sandbox_elodie_weider/Domain_2/1'>domain 2</scene>: residues 286-515		* <scene name='Sandbox_elodie_weider/Domain_2/1'>domain 2</scene>: residues 286-515

Élodie Weider at 18:09, 12 November 2009

Élodie Weider — Thu, 12 Nov 2009 18:09:23 GMT

←Older revision		Revision as of 18:09, 12 November 2009
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	== Introduction ==		== Introduction ==

-	Insulin-Degrading Enzyme ~~(IDE or insulinase or insulysin)~~ is a highly conserved ~~113~~ kDa zinc metalloprotease. It belongs to the M16A family of metalloproteases within the ME clan. It hydrolyses insulin and several amyloidogenic peptides like amyloid-β (Aβ).	+	Insulin-Degrading Enzyme is a highly conserved 226 kDa dimeric zinc metalloprotease. It belongs to the M16A family of metalloproteases within the ME clan. It hydrolyses insulin and several amyloidogenic peptides like amyloid-β (Aβ).
	Aβ is the main component of brain and of the amyloid islets found in Alzheimer’s disease.		Aβ is the main component of brain and of the amyloid islets found in Alzheimer’s disease.
	Insulin is a peptide associated with diabete. The gene encoding IDE is located on human chromosome 10q and is in a region linked to type 2 diabete and Alzheimer’s disease.		Insulin is a peptide associated with diabete. The gene encoding IDE is located on human chromosome 10q and is in a region linked to type 2 diabete and Alzheimer’s disease.

Élodie Weider at 17:55, 12 November 2009

Élodie Weider — Thu, 12 Nov 2009 17:55:23 GMT

←Older revision		Revision as of 17:55, 12 November 2009
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	* <scene name='Sandbox_elodie_weider/Domain_4/1'>domain 4</scene>: residues 769-1,016		* <scene name='Sandbox_elodie_weider/Domain_4/1'>domain 4</scene>: residues 769-1,016
	These domains share less than 25 % sequence similarity, and show similar secondary structures.		These domains share less than 25 % sequence similarity, and show similar secondary structures.
-	The N-terminal domains 1 and 2 form a αβαβα sandwich (<scene name='Sandbox_elodie_weider/Ide-n/1'>IDE-N</scene>), as do domains 3 and 4 (IDE-C). The size of each IDE-N and IDE-C is about 56 kDa.	+	The N-terminal domains 1 and 2 form a αβαβα sandwich (<scene name='Sandbox_elodie_weider/Ide-n/1'>IDE-N</scene>), as do domains 3 and 4 (<scene name='Sandbox_elodie_weider/Ide-c/1'>IDE-C</scene>). The size of each IDE-N and IDE-C is about 56 kDa.
	They are joined by a <scene name='Sandbox_elodie_weider/Loop/1'>26-residue loop</scene> (residues 516-541) which interacts with both domains 2 and 3, but not with domains 1 and 4.		They are joined by a <scene name='Sandbox_elodie_weider/Loop/1'>26-residue loop</scene> (residues 516-541) which interacts with both domains 2 and 3, but not with domains 1 and 4.
	There is an extensive interaction between IDE-N and IDE-C domains, that bury a large surface ( 11,200 Ȧ<sup>2</sup>), with good shape complementarity. This interaction between the two domains of IDE is mediated by charge complementarity and Van der Waals interactions.		There is an extensive interaction between IDE-N and IDE-C domains, that bury a large surface ( 11,200 Ȧ<sup>2</sup>), with good shape complementarity. This interaction between the two domains of IDE is mediated by charge complementarity and Van der Waals interactions.

Élodie Weider at 17:52, 12 November 2009

Élodie Weider — Thu, 12 Nov 2009 17:52:45 GMT

←Older revision		Revision as of 17:52, 12 November 2009
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	* <scene name='Sandbox_elodie_weider/Domain_4/1'>domain 4</scene>: residues 769-1,016		* <scene name='Sandbox_elodie_weider/Domain_4/1'>domain 4</scene>: residues 769-1,016
	These domains share less than 25 % sequence similarity, and show similar secondary structures.		These domains share less than 25 % sequence similarity, and show similar secondary structures.
-	The N-terminal domains 1 and 2 form a αβαβα sandwich (IDE-N), as do domains 3 and 4 (IDE-C). The size of each IDE-N and IDE-C is about 56 kDa.	+	The N-terminal domains 1 and 2 form a αβαβα sandwich (<scene name='Sandbox_elodie_weider/Ide-n/1'>IDE-N</scene>), as do domains 3 and 4 (IDE-C). The size of each IDE-N and IDE-C is about 56 kDa.
	They are joined by a <scene name='Sandbox_elodie_weider/Loop/1'>26-residue loop</scene> (residues 516-541) which interacts with both domains 2 and 3, but not with domains 1 and 4.		They are joined by a <scene name='Sandbox_elodie_weider/Loop/1'>26-residue loop</scene> (residues 516-541) which interacts with both domains 2 and 3, but not with domains 1 and 4.
	There is an extensive interaction between IDE-N and IDE-C domains, that bury a large surface ( 11,200 Ȧ<sup>2</sup>), with good shape complementarity. This interaction between the two domains of IDE is mediated by charge complementarity and Van der Waals interactions.		There is an extensive interaction between IDE-N and IDE-C domains, that bury a large surface ( 11,200 Ȧ<sup>2</sup>), with good shape complementarity. This interaction between the two domains of IDE is mediated by charge complementarity and Van der Waals interactions.

Élodie Weider at 17:48, 12 November 2009

Élodie Weider — Thu, 12 Nov 2009 17:48:41 GMT

←Older revision		Revision as of 17:48, 12 November 2009
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	These domains share less than 25 % sequence similarity, and show similar secondary structures.		These domains share less than 25 % sequence similarity, and show similar secondary structures.
	The N-terminal domains 1 and 2 form a αβαβα sandwich (IDE-N), as do domains 3 and 4 (IDE-C). The size of each IDE-N and IDE-C is about 56 kDa.		The N-terminal domains 1 and 2 form a αβαβα sandwich (IDE-N), as do domains 3 and 4 (IDE-C). The size of each IDE-N and IDE-C is about 56 kDa.
-	They are joined by a 26-residue loop (residues 516-541) which interacts with both domains 2 and 3, but not with domains 1 and 4.	+	They are joined by a <scene name='Sandbox_elodie_weider/Loop/1'>26-residue loop</scene> (residues 516-541) which interacts with both domains 2 and 3, but not with domains 1 and 4.
	There is an extensive interaction between IDE-N and IDE-C domains, that bury a large surface ( 11,200 Ȧ<sup>2</sup>), with good shape complementarity. This interaction between the two domains of IDE is mediated by charge complementarity and Van der Waals interactions.		There is an extensive interaction between IDE-N and IDE-C domains, that bury a large surface ( 11,200 Ȧ<sup>2</sup>), with good shape complementarity. This interaction between the two domains of IDE is mediated by charge complementarity and Van der Waals interactions.
	IDE-C plays also is also involved in the oligomerization of IDE.		IDE-C plays also is also involved in the oligomerization of IDE.

Élodie Weider at 17:37, 12 November 2009

Élodie Weider — Thu, 12 Nov 2009 17:37:54 GMT

←Older revision		Revision as of 17:37, 12 November 2009
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	* <scene name='Sandbox_elodie_weider/Domain_2/1'>domain 2</scene>: residues 286-515		* <scene name='Sandbox_elodie_weider/Domain_2/1'>domain 2</scene>: residues 286-515
	* <scene name='Sandbox_elodie_weider/Domain_3/1'>domain 3</scene>: residues 542-768		* <scene name='Sandbox_elodie_weider/Domain_3/1'>domain 3</scene>: residues 542-768
-	* domain 4: residues 769-1,016	+	* <scene name='Sandbox_elodie_weider/Domain_4/1'>domain 4</scene>: residues 769-1,016
	These domains share less than 25 % sequence similarity, and show similar secondary structures.		These domains share less than 25 % sequence similarity, and show similar secondary structures.
	The N-terminal domains 1 and 2 form a αβαβα sandwich (IDE-N), as do domains 3 and 4 (IDE-C). The size of each IDE-N and IDE-C is about 56 kDa.		The N-terminal domains 1 and 2 form a αβαβα sandwich (IDE-N), as do domains 3 and 4 (IDE-C). The size of each IDE-N and IDE-C is about 56 kDa.

Élodie Weider at 17:35, 12 November 2009

Élodie Weider — Thu, 12 Nov 2009 17:35:37 GMT

←Older revision		Revision as of 17:35, 12 November 2009
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	* <scene name='Sandbox_elodie_weider/Domain_1/2'>domain 1</scene>: residues 43-285		* <scene name='Sandbox_elodie_weider/Domain_1/2'>domain 1</scene>: residues 43-285
	* <scene name='Sandbox_elodie_weider/Domain_2/1'>domain 2</scene>: residues 286-515		* <scene name='Sandbox_elodie_weider/Domain_2/1'>domain 2</scene>: residues 286-515
-	* domain 3: residues 542-768	+	* <scene name='Sandbox_elodie_weider/Domain_3/1'>domain 3</scene>: residues 542-768
	* domain 4: residues 769-1,016		* domain 4: residues 769-1,016
	These domains share less than 25 % sequence similarity, and show similar secondary structures.		These domains share less than 25 % sequence similarity, and show similar secondary structures.

Élodie Weider at 17:33, 12 November 2009

Élodie Weider — Thu, 12 Nov 2009 17:33:17 GMT

←Older revision		Revision as of 17:33, 12 November 2009
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	IDE is a dimeric protein. Each IDE monomer is composed of four 25-27 kDa structurally homologous αβ roll domains:		IDE is a dimeric protein. Each IDE monomer is composed of four 25-27 kDa structurally homologous αβ roll domains:
	* <scene name='Sandbox_elodie_weider/Domain_1/2'>domain 1</scene>: residues 43-285		* <scene name='Sandbox_elodie_weider/Domain_1/2'>domain 1</scene>: residues 43-285
-	* domain 2: residues 286-515	+	* <scene name='Sandbox_elodie_weider/Domain_2/1'>domain 2</scene>: residues 286-515
	* domain 3: residues 542-768		* domain 3: residues 542-768
	* domain 4: residues 769-1,016		* domain 4: residues 769-1,016

Élodie Weider at 17:30, 12 November 2009

Élodie Weider — Thu, 12 Nov 2009 17:30:43 GMT

←Older revision		Revision as of 17:30, 12 November 2009
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	IDE is a dimeric protein. Each IDE monomer is composed of four 25-27 kDa structurally homologous αβ roll domains:		IDE is a dimeric protein. Each IDE monomer is composed of four 25-27 kDa structurally homologous αβ roll domains:
-	* domain 1: residues 43-285	+	* <scene name='Sandbox_elodie_weider/Domain_1/2'>domain 1</scene>: residues 43-285
	* domain 2: residues 286-515		* domain 2: residues 286-515
	* domain 3: residues 542-768		* domain 3: residues 542-768