1alw

<StructureSection load='1alw' size='340' side='right' caption='[[1alw]], [[Resolution|resolution]] 2.03&Aring;' scene=''>

<table><tr><td colspan='2'>[[1alw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ALW FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ISA:3-(4-IODO-PHENYL)-2-MERCAPTO-PROPIONIC+ACID'>ISA</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1alw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1alw RCSB], [http://www.ebi.ac.uk/pdbsum/1alw PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/CPNS1_PIG CPNS1_PIG]] Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/al/1alw_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:9228946</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1alw" style="background-color:#fffaf0;"></div>

*[[Calpain|Calpain]]

[[Category: Pig]]

[[Category: Lin, G]]

[[Category: Narayana, S V.L]]

[[Category: Calcium binding]]

[[Category: Domain of cystein protease]]