Sandbox Reserved 954: Difference between revisions

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STRUCTURALLY SIMILAR BUT FUNCTIONALLY DIVERSE PROTEINShttp://www.jbc.org/content/early/2001/07/02/jbc.R100016200.full.pdf DOI : 2001/07/02/jbc.R100016200.full.pdf </ref>

SerpinB3 means serin protease inhibitor, clade B (ovalbumin), member 3. The particularity of Serpin B3 is to target proteases wich have a nucleophilic cysteine instead of serine in their catalytic site.

SCCA1 is a trimeric protein. Like all for serpins, <scene name='60/604473/One_subunit/1'>one subunit</scene> has three β sheets termed <scene name='60/604473/A_beta_sheet/3'>A (7 stranded)</scene>, <scene name='60/604473/B_beta_sheet/2'>B (5 stranded)</scene> and <scene name='60/604473/C_beta_sheet/2'>C (6 stranded)</scene> and <scene name='60/604473/Alpha_helices/1'>11 α helices (hA to hK)</scene>. <ref>~~PMDI~~ : ~~19166818~~ </ref>

SCCA1 is a trimeric protein<ref> PMID : 19166818 </ref>

. Like all for serpins, <scene name='60/604473/One_subunit/1'>one subunit</scene> has three β sheets termed <scene name='60/604473/A_beta_sheet/3'>A (7 stranded)</scene>, <scene name='60/604473/B_beta_sheet/2'>B (5 stranded)</scene> and <scene name='60/604473/C_beta_sheet/2'>C (6 stranded)</scene> and <scene name='60/604473/Alpha_helices/1'>11 α helices (hA to hK)</scene> <ref>Gary A. Silverman1*, Phillip I. Bird2

The most important part of Serpins is an exposed region of 20 amino acids near the C terminus named the reactive center loop (<scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene>). This <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> allow the specificity interaction of the inhibitor for the target protease<ref>PMID : PMC24842</ref>.

, Robin W. Carrell3

, Frank C. Church4

, Paul B. Coughlin5

, Peter G.W. Gettins6

,

James A Irving2

, David A. Lomas3

, Cliff J. Luke1

, Richard W. Moyer7

, Philip A. Pemberton8

, Eileen RemoldO'Donnell9

, Guy S. Salvesen10, James Travis11 and James C. Whisstock, THE SERPINS ARE AN EXPANDING SUPERFAMILY OF

STRUCTURALLY SIMILAR BUT FUNCTIONALLY DIVERSE PROTEINS, http://www.jbc.org/content/early/2001/07/02/jbc.R100016200.full.pdf DOI : 2001/07/02/jbc.R100016200.full.pdf </ref> <ref>PDB, Crystal structure of human squamous cell carcinoma antigen 1 http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=2ZV6&bionumber=1 DOI : pdb/explore/remediatedSequence.do?structureId=2ZV6&bionumber=1</ref> .

The most important part of Serpins is an exposed region of 20 amino acids near the C terminus named the reactive center loop (<scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene>). This <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> allow the specificity interaction of the inhibitor for the target protease<ref> PMID : PMC24842</ref>.

[[Image:Structure region.jpg|400px]]

Sandbox Reserved 954: Difference between revisions

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@@ Line 15: / Line 15: @@
 STRUCTURALLY SIMILAR BUT FUNCTIONALLY DIVERSE PROTEINShttp://www.jbc.org/content/early/2001/07/02/jbc.R100016200.full.pdf DOI : 2001/07/02/jbc.R100016200.full.pdf </ref>
 SerpinB3 means serin protease inhibitor, clade B (ovalbumin), member 3. The particularity of Serpin B3 is to target proteases wich have a nucleophilic cysteine instead of serine in their catalytic site.
-SCCA1 is a trimeric protein. Like all for serpins, <scene name='60/604473/One_subunit/1'>one subunit</scene> has three β sheets termed <scene name='60/604473/A_beta_sheet/3'>A (7 stranded)</scene>, <scene name='60/604473/B_beta_sheet/2'>B (5 stranded)</scene> and <scene name='60/604473/C_beta_sheet/2'>C (6 stranded)</scene> and <scene name='60/604473/Alpha_helices/1'>11  α helices (hA to hK)</scene>. <ref>PMDI : 19166818 </ref>
+SCCA1 is a trimeric protein<ref> PMID : 19166818 </ref>
+. Like all for serpins, <scene name='60/604473/One_subunit/1'>one subunit</scene> has three β sheets termed <scene name='60/604473/A_beta_sheet/3'>A (7 stranded)</scene>, <scene name='60/604473/B_beta_sheet/2'>B (5 stranded)</scene> and <scene name='60/604473/C_beta_sheet/2'>C (6 stranded)</scene> and <scene name='60/604473/Alpha_helices/1'>11  α helices (hA to hK)</scene> <ref>Gary A. Silverman1*, Phillip I. Bird2
-The most important part of Serpins is an exposed region of 20 amino acids near the C terminus named the reactive center loop (<scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene>). This <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> allow the specificity interaction of the inhibitor for the target protease<ref>PMID : PMC24842</ref>.
+, Robin W. Carrell3
+, Frank C. Church4
+, Paul B. Coughlin5
+, Peter G.W. Gettins6
+,
+James A Irving2
+, David A. Lomas3
+, Cliff J. Luke1
+, Richard W. Moyer7
+, Philip A. Pemberton8
+, Eileen RemoldO'Donnell9
+, Guy S. Salvesen10, James Travis11 and James C. Whisstock, THE SERPINS ARE AN EXPANDING SUPERFAMILY OF
+STRUCTURALLY SIMILAR BUT FUNCTIONALLY DIVERSE PROTEINS, http://www.jbc.org/content/early/2001/07/02/jbc.R100016200.full.pdf DOI : 2001/07/02/jbc.R100016200.full.pdf </ref> <ref>PDB, Crystal structure of human squamous cell carcinoma antigen 1 http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=2ZV6&bionumber=1 DOI : pdb/explore/remediatedSequence.do?structureId=2ZV6&bionumber=1</ref> .
+The most important part of Serpins is an exposed region of 20 amino acids near the C terminus named the reactive center loop (<scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene>). This <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> allow the specificity interaction of the inhibitor for the target protease<ref> PMID : PMC24842</ref>.
 [[Image:Structure region.jpg|400px]]