Sandbox16: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
Student (talk | contribs)
students
33,923 edits
No edit summary
Student (talk | contribs)
students
33,923 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
Protein: human Beta secretase complexed with inhibitor (1tqf)
{{STRUCTURE_1tqf |  PDB=1tqf  |  SCENE=  }}
 
===Protein: human Beta secretase complexed with inhibitor (1tqf)===
By Amit Shavit and Nikola Finneran
By Amit Shavit and Nikola Finneran
 
 
 
<br>
==Protein==
==Protein==


A small molecule nonpeptide inhibitor of beta-secretase has been developed, and its binding has been defined through crystallographic determination of the enzyme-inhibitor complex. The molecule is shown to bind to the catalytic aspartate residues in an unprecedented manner in the field of aspartyl protease inhibition. Additionally, the complex reveals a heretofore unknown S(3) subpocket that is created by the inhibitor. This structure has served an important role in the design of newer beta-secretase inhibitors. (http://www.proteopedia.org/wiki/index.php/1tqf)
A small molecule nonpeptide inhibitor of beta-secretase has been developed, and its binding has been defined through crystallographic determination of the enzyme-inhibitor complex. The molecule is shown to bind to the catalytic aspartate residues in an unprecedented manner in the field of aspartyl protease inhibition. Additionally, the complex reveals a heretofore unknown S(3) subpocket that is created by the inhibitor. This structure has served an important role in the design of newer beta-secretase inhibitors. (http://www.proteopedia.org/wiki/index.php/1tqf)


==Structure==
==Structure==
Our protein is mostly composed of <scene name='Sandbox16/Mynewscene/1'>alpha helices</scene> (shown in red) and <scene name='Sandbox16/Mynewscene1/1'>beta sheets</scene> (shown in blue) which contain some of the <scene name='Sandbox16/Mynewscene2/1'>hydrophobic regions</scene> (shown in purple). The <scene name='Sandbox16/Mynewscene3/1'>ligand</scene> in the center is highlighted in yellow.
Our protein is mostly composed of <scene name='Sandbox16/Mynewscene/1'>alpha helices</scene> (shown in red) and <scene name='Sandbox16/Mynewscene1/1'>beta sheets</scene> (shown in blue) which contain some of the <scene name='Sandbox16/Mynewscene2/1'>hydrophobic regions</scene> (shown in purple). The <scene name='Sandbox16/Mynewscene4/1'>ligand</scene> in the center is highlighted in yellow.


==References==
Identification of a small molecule nonpeptide active site beta-secretase inhibitor that displays a nontraditional binding mode for aspartyl proteases., Coburn CA, Stachel SJ, Li YM, Rush DM, Steele TG, Chen-Dodson E, Holloway MK, Xu M, Huang Q, Lai MT, DiMuzio J, Crouthamel MC, Shi XP, Sardana V, Chen Z, Munshi S, Kuo L, Makara GM, Annis DA, Tadikonda PK, Nash HM, Vacca JP, Wang T, J Med Chem. 2004 Dec 2;47(25):6117-9. PMID:15566281


Reference: Identification of a small molecule nonpeptide active site beta-secretase inhibitor that displays a nontraditional binding mode for aspartyl proteases., Coburn CA, Stachel SJ, Li YM, Rush DM, Steele TG, Chen-Dodson E, Holloway MK, Xu M, Huang Q, Lai MT, DiMuzio J, Crouthamel MC, Shi XP, Sardana V, Chen Z, Munshi S, Kuo L, Makara GM, Annis DA, Tadikonda PK, Nash HM, Vacca JP, Wang T, J Med Chem. 2004 Dec 2;47(25):6117-9. PMID:15566281
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
 
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.  
 
 
{{STRUCTURE_1tqf |  PDB=1tqf  |  SCENE=  }}

Latest revision as of 16:46, 4 March 2009

Drag the structure with the mouse to rotate
1tqf, resolution 1.80Å (default scene)
Ligands: 32P
Gene: BACE1, BACE (Homo sapiens)
Activity: Memapsin 2, with EC number 3.4.23.46
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml


Protein: human Beta secretase complexed with inhibitor (1tqf)

By Amit Shavit and Nikola Finneran


Protein

A small molecule nonpeptide inhibitor of beta-secretase has been developed, and its binding has been defined through crystallographic determination of the enzyme-inhibitor complex. The molecule is shown to bind to the catalytic aspartate residues in an unprecedented manner in the field of aspartyl protease inhibition. Additionally, the complex reveals a heretofore unknown S(3) subpocket that is created by the inhibitor. This structure has served an important role in the design of newer beta-secretase inhibitors. (https://www.proteopedia.org/wiki/index.php/1tqf)


Structure

Our protein is mostly composed of alpha helices (shown in red) and beta sheets (shown in blue) which contain some of the hydrophobic regions (shown in purple). The ligand in the center is highlighted in yellow.

References

Identification of a small molecule nonpeptide active site beta-secretase inhibitor that displays a nontraditional binding mode for aspartyl proteases., Coburn CA, Stachel SJ, Li YM, Rush DM, Steele TG, Chen-Dodson E, Holloway MK, Xu M, Huang Q, Lai MT, DiMuzio J, Crouthamel MC, Shi XP, Sardana V, Chen Z, Munshi S, Kuo L, Makara GM, Annis DA, Tadikonda PK, Nash HM, Vacca JP, Wang T, J Med Chem. 2004 Dec 2;47(25):6117-9. PMID:15566281

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Retrieved from "https://proteopedia.org/index.php?title=Sandbox16&oldid=934107"