1jqp: Difference between revisions

New page: left|200px<br /><applet load="1jqp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jqp, resolution 2.4Å" /> '''dipeptidyl peptidase ...
 
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[[Image:1jqp.jpg|left|200px]]<br /><applet load="1jqp" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1jqp.jpg|left|200px]]<br /><applet load="1jqp" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jqp, resolution 2.4&Aring;" />
caption="1jqp, resolution 2.4&Aring;" />
'''dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family'''<br />
'''dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family'''<br />


==Overview==
==Overview==
The crystal structure of mature dipeptidyl peptidase I reveals insight, into the unique tetrameric structure, substrate binding and activation of, this atypical papain family peptidase. Each subunit is composed of three, peptides. The heavy and light chains form the catalytic domain, which, adopts the papain fold. The residual pro-part forms a beta-barrel with the, carboxylate group of Asp1 pointing towards the substrate amino-terminus., The tetrameric structure appears to stabilize the association of the two, domains and encloses a 12700 A3 spherical cavity. The tetramer contains, six chloride ions, one buried in each S2 pocket and two at subunit, interfaces.
The crystal structure of mature dipeptidyl peptidase I reveals insight into the unique tetrameric structure, substrate binding and activation of this atypical papain family peptidase. Each subunit is composed of three peptides. The heavy and light chains form the catalytic domain, which adopts the papain fold. The residual pro-part forms a beta-barrel with the carboxylate group of Asp1 pointing towards the substrate amino-terminus. The tetrameric structure appears to stabilize the association of the two domains and encloses a 12700 A3 spherical cavity. The tetramer contains six chloride ions, one buried in each S2 pocket and two at subunit interfaces.


==About this Structure==
==About this Structure==
1JQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NAG, CL and SO4 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JQP OCA].  
1JQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] 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=1JQP OCA].  


==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Dahl, S.W.]]
[[Category: Dahl, S W.]]
[[Category: Kadziola, A.]]
[[Category: Kadziola, A.]]
[[Category: Larsen, S.]]
[[Category: Larsen, S.]]
[[Category: Lauritzen, C.]]
[[Category: Lauritzen, C.]]
[[Category: Olsen, J.G.]]
[[Category: Olsen, J G.]]
[[Category: Pedersen, J.]]
[[Category: Pedersen, J.]]
[[Category: CL]]
[[Category: CL]]
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[[Category: tetramer]]
[[Category: tetramer]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:29:30 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:39 2008''

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