4bw8
From Proteopedia
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| - | + | ==Calmodulin with small bend in central helix== | |
| - | ===Calmodulin with | + | <StructureSection load='4bw8' size='340' side='right' caption='[[4bw8]], [[Resolution|resolution]] 1.80Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4bw8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BW8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BW8 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></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bw7|4bw7]]</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=4bw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bw8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bw8 RCSB], [http://www.ebi.ac.uk/pdbsum/4bw8 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Calmodulin is one of the most well characterized proteins and a widely used model system for calcium binding and large-scale protein conformational changes. Its long central helix is usually cut in half when a target peptide is bound. Here, two new crystal structures of calmodulin are presented, in which conformations possibly representing the first steps of calmodulin conformational collapse have been trapped. The central helix in the two structures is bent in the middle, causing a significant movement of the N- and C-terminal lobes with respect to one another. In both of the bent structures, a nearby polar side chain is inserted into the helical groove, disrupting backbone hydrogen bonding. The structures give an insight into the details of the factors that may be involved in the distortion of the central helix upon ligand peptide binding. | ||
| - | + | Crystallographic snapshots of initial steps in the collapse of the calmodulin central helix.,Kursula P Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):24-30. doi:, 10.1107/S1399004713024437. Epub 2013 Dec 24. PMID:24419375<ref>PMID:24419375</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Kursula, P | + | |
| + | ==See Also== | ||
| + | *[[Calmodulin|Calmodulin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Kursula, P]] | ||
[[Category: Metal binding protein]] | [[Category: Metal binding protein]] | ||
Revision as of 18:40, 21 December 2014
Calmodulin with small bend in central helix
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