1k3b: Difference between revisions

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[[Image:1k3b.jpg|left|200px]]<br /><applet load="1k3b" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1k3b.jpg|left|200px]]
caption="1k3b, resolution 2.15&Aring;" />
 
'''Crystal Structure of Human Dipeptidyl Peptidase I (Cathepsin C): Exclusion Domain Added to an Endopeptidase Framework Creates the Machine for Activation of Granular Serine Proteases'''<br />
{{Structure
|PDB= 1k3b |SIZE=350|CAPTION= <scene name='initialview01'>1k3b</scene>, resolution 2.15&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=
}}
 
'''Crystal Structure of Human Dipeptidyl Peptidase I (Cathepsin C): Exclusion Domain Added to an Endopeptidase Framework Creates the Machine for Activation of Granular Serine Proteases'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1K3B 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=1K3B OCA].  
1K3B 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=1K3B OCA].  


==Reference==
==Reference==
Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases., Turk D, Janjic V, Stern I, Podobnik M, Lamba D, Dahl SW, Lauritzen C, Pedersen J, Turk V, Turk B, EMBO J. 2001 Dec 3;20(23):6570-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11726493 11726493]
Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases., Turk D, Janjic V, Stern I, Podobnik M, Lamba D, Dahl SW, Lauritzen C, Pedersen J, Turk V, Turk B, EMBO J. 2001 Dec 3;20(23):6570-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11726493 11726493]
[[Category: Dipeptidyl-peptidase I]]
[[Category: Dipeptidyl-peptidase I]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: hydrolase]]
[[Category: hydrolase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:47 2008''
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Revision as of 13:12, 20 March 2008

File:1k3b.jpg


PDB ID 1k3b

Drag the structure with the mouse to rotate
, resolution 2.15Å
Ligands: , and
Activity: Dipeptidyl-peptidase I, with EC number 3.4.14.1
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Human Dipeptidyl Peptidase I (Cathepsin C): Exclusion Domain Added to an Endopeptidase Framework Creates the Machine for Activation of Granular Serine Proteases


OverviewOverview

Dipeptidyl peptidase I (DPPI) or cathepsin C is the physiological activator of groups of serine proteases from immune and inflammatory cells vital for defense of an organism. The structure presented shows how an additional domain transforms the framework of a papain-like endopeptidase into a robust oligomeric protease-processing enzyme. The tetrahedral arrangement of the active sites exposed to solvent allows approach of proteins in their native state; the massive body of the exclusion domain fastened within the tetrahedral framework excludes approach of a polypeptide chain apart from its termini; and the carboxylic group of Asp1 positions the N-terminal amino group of the substrate. Based on a structural comparison and interactions within the active site cleft, it is suggested that the exclusion domain originates from a metallo-protease inhibitor. The location of missense mutations, characterized in people suffering from Haim-Munk and Papillon-Lefevre syndromes, suggests how they disrupt the fold and function of the enzyme.

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

1K3B is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases., Turk D, Janjic V, Stern I, Podobnik M, Lamba D, Dahl SW, Lauritzen C, Pedersen J, Turk V, Turk B, EMBO J. 2001 Dec 3;20(23):6570-82. PMID:11726493

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