1vbs

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[[Image:1vbs.gif|left|200px]]
[[Image:1vbs.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1vbs |SIZE=350|CAPTION= <scene name='initialview01'>1vbs</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1vbs", 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=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=NIT:4-NITROANILINE'>NIT</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=
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or leave the SCENE parameter empty for the default display.
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|GENE= CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_1vbs| PDB=1vbs | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vbs OCA], [http://www.ebi.ac.uk/pdbsum/1vbs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vbs RCSB]</span>
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}}
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'''STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)ALA CONTAINING TETRAPEPTIDE'''
'''STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)ALA CONTAINING TETRAPEPTIDE'''
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[[Category: Schutkowski, M.]]
[[Category: Schutkowski, M.]]
[[Category: Zhao, Y.]]
[[Category: Zhao, Y.]]
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[[Category: competitive inhibitor]]
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[[Category: Competitive inhibitor]]
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[[Category: complex (isomerase/peptide)]]
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[[Category: Cyclophilin some]]
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[[Category: cyclophilin some]]
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[[Category: Mechanism]]
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[[Category: mechanism]]
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[[Category: Peptidyl-prolyl isomerase]]
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[[Category: peptidyl-prolyl isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:20:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:22:10 2008''
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Revision as of 09:20, 3 May 2008

Template:STRUCTURE 1vbs

STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)ALA CONTAINING TETRAPEPTIDE


Overview

The stereospecificity of peptidyl prolyl cis/trans isomerases (PPIases) was studied using tetrapeptide substrate analogs in which one amino acid residue was replaced by the cognate D-amino acid in various positions of the peptide chain. Reversed stereocenters around proline markedly increased the rate of the spontaneous trans to cis isomerization of the prolyl bond whereas cis to trans isomerizations were less sensitive. PPIases like human cyclophilin18, human FKBP12, Escherichia coli parvulin10 and the PPIase domain of E. coli trigger factor exhibited stereoselectivity demanding at the P1 to P2' position of the substrate chain. The discriminating factor for stereoselectivity was the lack of formation of the Michaelis complexes of the diastereomeric substrates. However, D-alanine at the P1 position preserved considerable affinity to the active site, and largely prevented activation of the catalytic machinery for all PPIases investigated.

About this Structure

1VBS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Mapping the stereospecificity of peptidyl prolyl cis/trans isomerases., Schiene C, Reimer U, Schutkowski M, Fischer G, FEBS Lett. 1998 Aug 7;432(3):202-6. PMID:9720925 Page seeded by OCA on Sat May 3 12:20:47 2008

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