2djg: Difference between revisions

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[[Image:2djg.gif|left|200px]]<br /><applet load="2djg" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2djg.gif|left|200px]]
caption="2djg, resolution 2.05&Aring;" />
 
'''Re-refinement of the native structure of human dipeptidyl peptidase I (cathepsin C)'''<br />
{{Structure
|PDB= 2djg |SIZE=350|CAPTION= <scene name='initialview01'>2djg</scene>, resolution 2.05&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_I Dipeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.1 3.4.14.1]
|GENE= CTSC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''Re-refinement of the native structure of human dipeptidyl peptidase I (cathepsin C)'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2DJG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_I Dipeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.1 3.4.14.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DJG OCA].  
2DJG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DJG OCA].  


==Reference==
==Reference==
The crystal structure of human dipeptidyl peptidase I (cathepsin C) in complex with the inhibitor Gly-Phe-CHN2., Molgaard A, Arnau J, Lauritzen C, Larsen S, Petersen G, Pedersen J, Biochem J. 2007 Feb 1;401(3):645-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17020538 17020538]
The crystal structure of human dipeptidyl peptidase I (cathepsin C) in complex with the inhibitor Gly-Phe-CHN2., Molgaard A, Arnau J, Lauritzen C, Larsen S, Petersen G, Pedersen J, Biochem J. 2007 Feb 1;401(3):645-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17020538 17020538]
[[Category: Dipeptidyl-peptidase I]]
[[Category: Dipeptidyl-peptidase I]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: re-refinement]]
[[Category: re-refinement]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:59:26 2008''
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Revision as of 17:27, 20 March 2008

File:2djg.gif


PDB ID 2djg

Drag the structure with the mouse to rotate
, resolution 2.05Å
Ligands: , and
Gene: CTSC (Homo sapiens)
Activity: Dipeptidyl-peptidase I, with EC number 3.4.14.1
Coordinates: save as pdb, mmCIF, xml



Re-refinement of the native structure of human dipeptidyl peptidase I (cathepsin C)


OverviewOverview

hDDPI (human dipeptidyl peptidase I) is a lysosomal cysteine protease involved in zymogen activation of granule-associated proteases, including granzymes A and B from cytotoxic T-lymphocytes and natural killer cells, cathepsin G and neutrophil elastase, and mast cell tryptase and chymase. In the present paper, we provide the first crystal structure of an hDPPI-inhibitor complex. The inhibitor Gly-Phe-CHN2 (Gly-Phe-diazomethane) was co-crystallized with hDPPI and the structure was determined at 2.0 A (1 A=0.1 nm) resolution. The structure of the native enzyme was also determined to 2.05 A resolution to resolve apparent discrepancies between the complex structure and the previously published structure of the native enzyme. The new structure of the native enzyme is, within the experimental error, identical with the structure of the enzyme-inhibitor complex presented here. The inhibitor interacts with three subunits of hDPPI, and is covalently bound to Cys234 at the active site. The interaction between the totally conserved Asp1 of hDPPI and the ammonium group of the inhibitor forms an essential interaction that mimics enzyme-substrate interactions. The structure of the inhibitor complex provides an explanation of the substrate specificity of hDPPI, and gives a background for the design of new inhibitors.

DiseaseDisease

Known diseases associated with this structure: Haim-Munk syndrome OMIM:[602365], Papillon-Lefevre syndrome OMIM:[602365], Periodontitis, juvenile OMIM:[602365]

About this StructureAbout this Structure

2DJG is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of human dipeptidyl peptidase I (cathepsin C) in complex with the inhibitor Gly-Phe-CHN2., Molgaard A, Arnau J, Lauritzen C, Larsen S, Petersen G, Pedersen J, Biochem J. 2007 Feb 1;401(3):645-50. PMID:17020538

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