1alw: Difference between revisions

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New page: left|200px<br /><applet load="1alw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1alw, resolution 2.03Å" /> '''INHIBITOR AND CALCIU...
 
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[[Image:1alw.gif|left|200px]]<br /><applet load="1alw" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1alw.gif|left|200px]]<br /><applet load="1alw" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1alw, resolution 2.03&Aring;" />
caption="1alw, resolution 2.03&Aring;" />
'''INHIBITOR AND CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN'''<br />
'''INHIBITOR AND CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN'''<br />


==Overview==
==Overview==
The three dimensional structure of calcium-bound domain VI of porcine, calpain has been determined to 1.9 A resolution. The crystal structure, reveals five EF-hands, one more than previously suggested. There are two, EF-hand pairs, one pair (EF1-EF2) displays an 'open' conformation and the, other (EF3-EF4) a 'closed' conformation. Unusually, a calcium atom is, found at the C-terminal end of the calcium binding loop of EF4. With two, additional residues in the calcium binding loop, the fifth EF-hand (EF5), is in a 'closed' conformation. EF5 pairs up with the corresponding fifth, EF-hand of a non-crystallographically related molecule. Considering the, EF5's role in a homodimer formation of domain VI, we suggest a model for, the assembly of heterodimeric calpain. The crystal structure of a Ca2+, bound domain VI-inhibitor (PD150606) complex has been refined to 2.1 A, resolution. A possible mode for calpain inhibition is discussed.
The three dimensional structure of calcium-bound domain VI of porcine calpain has been determined to 1.9 A resolution. The crystal structure reveals five EF-hands, one more than previously suggested. There are two EF-hand pairs, one pair (EF1-EF2) displays an 'open' conformation and the other (EF3-EF4) a 'closed' conformation. Unusually, a calcium atom is found at the C-terminal end of the calcium binding loop of EF4. With two additional residues in the calcium binding loop, the fifth EF-hand (EF5) is in a 'closed' conformation. EF5 pairs up with the corresponding fifth EF-hand of a non-crystallographically related molecule. Considering the EF5's role in a homodimer formation of domain VI, we suggest a model for the assembly of heterodimeric calpain. The crystal structure of a Ca2+ bound domain VI-inhibitor (PD150606) complex has been refined to 2.1 A resolution. A possible mode for calpain inhibition is discussed.


==About this Structure==
==About this Structure==
1ALW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA and ISA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.52 and 3.4.22.53 3.4.22.52 and 3.4.22.53] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ALW OCA].  
1ALW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ISA:'>ISA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.52 and 3.4.22.53 3.4.22.52 and 3.4.22.53] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALW OCA].  


==Reference==
==Reference==
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Lin, G.]]
[[Category: Lin, G.]]
[[Category: Narayana, S.V.L.]]
[[Category: Narayana, S V.L.]]
[[Category: CA]]
[[Category: CA]]
[[Category: ISA]]
[[Category: ISA]]
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[[Category: domain of cystein protease]]
[[Category: domain of cystein protease]]


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