1alw
From Proteopedia
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|PDB= 1alw |SIZE=350|CAPTION= <scene name='initialview01'>1alw</scene>, resolution 2.03Å | |PDB= 1alw |SIZE=350|CAPTION= <scene name='initialview01'>1alw</scene>, resolution 2.03Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ISA:3-(4-IODO-PHENYL)-2-MERCAPTO-PROPIONIC+ACID'>ISA</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1alw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alw OCA], [http://www.ebi.ac.uk/pdbsum/1alw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1alw RCSB]</span> | ||
}} | }} | ||
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[[Category: Lin, G.]] | [[Category: Lin, G.]] | ||
[[Category: Narayana, S V.L.]] | [[Category: Narayana, S V.L.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: ISA]] | ||
[[Category: calcium binding]] | [[Category: calcium binding]] | ||
[[Category: calmodulin like]] | [[Category: calmodulin like]] | ||
[[Category: domain of cystein protease]] | [[Category: domain of cystein protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:42:57 2008'' |
Revision as of 15:42, 30 March 2008
| |||||||
| , resolution 2.03Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Hydrolase, with EC number and 3.4.22.53 3.4.22.52 and 3.4.22.53 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
INHIBITOR AND 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
1ALW is a Single protein structure of sequence from Sus scrofa. 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
Page seeded by OCA on Sun Mar 30 18:42:57 2008
