2n77: Difference between revisions
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==NMR solution structure of a complex of PEP-19 bound to the C-domain of apo calmodulin== | |||
<StructureSection load='2n77' size='340' side='right' caption='[[2n77]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2n77]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N77 FirstGlance]. <br> | |||
</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=2n77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n77 OCA], [http://pdbe.org/2n77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n77 RCSB], [http://www.ebi.ac.uk/pdbsum/2n77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n77 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/PCP4_HUMAN PCP4_HUMAN]] Probable regulator of calmodulin signaling.<ref>PMID:19106096</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
PEP-19 is a small protein that increases the rates of Ca2+ binding to the C-domain of calmodulin (CaM) by an unknown mechanism. Although an IQ motif promotes binding to CaM, an acidic sequence in PEP-19 is required to modulate Ca2+ binding and to sensitize HeLa cells to ATP-induced Ca2+ release. Here, we report the NMR solution structure of a complex between PEP-19 and the C-domain of apo CaM. The acidic sequence of PEP-19 associates between helices E and F of CaM via hydrophobic interactions. This allows the acidic side chains in PEP-19 to extend toward the solvent and form a negatively charged surface that resembles a catcher's mitt near Ca2+ binding loop III of CaM. The topology and gradients of negative electrostatic surface potential support a mechanism by which PEP-19 increases the rate of Ca2+ binding to the C-domain of CaM by 'catching' and electrostatically steering Ca2+ to site III. | |||
PEP-19 modulates calcium binding to calmodulin by electrostatic steering.,Wang X, Putkey JA Nat Commun. 2016 Nov 23;7:13583. doi: 10.1038/ncomms13583. PMID:27876793<ref>PMID:27876793</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Putkey, J | <div class="pdbe-citations 2n77" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Putkey, J A]] | |||
[[Category: Wang, X]] | [[Category: Wang, X]] | ||
[[Category: Intrinsically disordered]] | |||
[[Category: Signaling protein]] | |||
[[Category: Structural transition]] | |||
Revision as of 19:40, 9 December 2016
NMR solution structure of a complex of PEP-19 bound to the C-domain of apo calmodulin
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