1alv

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(New page: 200px<br /><applet load="1alv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1alv, resolution 1.9&Aring;" /> '''CALCIUM BOUND DOMAIN ...)
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[[Image:1alv.gif|left|200px]]<br /><applet load="1alv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1alv, resolution 1.9&Aring;" />
caption="1alv, resolution 1.9&Aring;" />
'''CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN'''<br />
'''CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN'''<br />
==Overview==
==Overview==
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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.
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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==
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1ALV 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1ALV OCA].
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1ALV 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> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1ALV OCA].
==Reference==
==Reference==
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[[Category: Lin, G.]]
[[Category: Lin, G.]]
[[Category: Maki, M.]]
[[Category: Maki, M.]]
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[[Category: Narayana, S.V.L.]]
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[[Category: Narayana, S V.L.]]
[[Category: CA]]
[[Category: CA]]
[[Category: calcium binding]]
[[Category: calcium binding]]
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[[Category: domain of cystein protease]]
[[Category: domain of cystein protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:57:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:54 2008''

Revision as of 09:45, 21 February 2008


1alv, resolution 1.9Å

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CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN

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.

About this Structure

1ALV is a Single protein structure of sequence from Sus scrofa with as ligand. Active as Hydrolase, with EC number and 3.4.22.53 3.4.22.52 and 3.4.22.53 Full crystallographic information is available from OCA.

Reference

Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding., Lin GD, Chattopadhyay D, Maki M, Wang KK, Carson M, Jin L, Yuen PW, Takano E, Hatanaka M, DeLucas LJ, Narayana SV, Nat Struct Biol. 1997 Jul;4(7):539-47. PMID:9228946

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