1g0v

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[[Image:1g0v.jpg|left|200px]]
[[Image:1g0v.jpg|left|200px]]
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{{Structure
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|PDB= 1g0v |SIZE=350|CAPTION= <scene name='initialview01'>1g0v</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1g0v", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] </span>
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{{STRUCTURE_1g0v| PDB=1g0v | SCENE= }}
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|RELATEDENTRY=[[1dpj|1DPJ]], [[1dp5|1DP5]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0v OCA], [http://www.ebi.ac.uk/pdbsum/1g0v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g0v RCSB]</span>
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'''THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT, MVV'''
'''THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT, MVV'''
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[[Category: Winther, J.]]
[[Category: Winther, J.]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
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[[Category: mvv]]
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[[Category: Mvv]]
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[[Category: proteinase some]]
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[[Category: Proteinase some]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:59:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:34:13 2008''
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Revision as of 13:59, 2 May 2008

Template:STRUCTURE 1g0v

THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT, MVV


Overview

The yeast IA3 polypeptide consists of only 68 residues, and the free inhibitor has little intrinsic secondary structure. IA3 showed subnanomolar potency toward its target, proteinase A from Saccharomyces cerevisiae, and did not inhibit any of a large number of aspartic proteinases with similar sequences/structures from a wide variety of other species. Systematic truncation and mutagenesis of the IA3 polypeptide revealed that the inhibitory activity is located in the N-terminal half of the sequence. Crystal structures of different forms of IA3 complexed with proteinase A showed that residues in the N-terminal half of the IA3 sequence became ordered and formed an almost perfect alpha-helix in the active site of the enzyme. This potent, specific interaction was directed primarily by hydrophobic interactions made by three key features in the inhibitory sequence. Whereas IA3 was cut as a substrate by the nontarget aspartic proteinases, it was not cleaved by proteinase A. The random coil IA3 polypeptide escapes cleavage by being stabilized in a helical conformation upon interaction with the active site of proteinase A. This results, paradoxically, in potent selective inhibition of the target enzyme.

About this Structure

1G0V is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae., Phylip LH, Lees WE, Brownsey BG, Bur D, Dunn BM, Winther JR, Gustchina A, Li M, Copeland T, Wlodawer A, Kay J, J Biol Chem. 2001 Jan 19;276(3):2023-30. Epub 2000 Oct 19. PMID:11042188 Page seeded by OCA on Fri May 2 16:59:30 2008

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