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| {{STRUCTURE_2be6| PDB=2be6 | SCENE= }} | | {{STRUCTURE_2be6| PDB=2be6 | SCENE= }} |
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| '''2.0 A crystal structure of the CaV1.2 IQ domain-Ca/CaM complex'''
| | ===2.0 A crystal structure of the CaV1.2 IQ domain-Ca/CaM complex=== |
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| ==Overview==
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| Changes in activity-dependent calcium flux through voltage-gated calcium channels (Ca(V)s) drive two self-regulatory calcium-dependent feedback processes that require interaction between Ca(2+)/calmodulin (Ca(2+)/CaM) and a Ca(V) channel consensus isoleucine-glutamine (IQ) motif: calcium-dependent inactivation (CDI) and calcium-dependent facilitation (CDF). Here, we report the high-resolution structure of the Ca(2+)/CaM-Ca(V)1.2 IQ domain complex. The IQ domain engages hydrophobic pockets in the N-terminal and C-terminal Ca(2+)/CaM lobes through sets of conserved 'aromatic anchors.' Ca(2+)/N lobe adopts two conformations that suggest inherent conformational plasticity at the Ca(2+)/N lobe-IQ domain interface. Titration calorimetry experiments reveal competition between the lobes for IQ domain sites. Electrophysiological examination of Ca(2+)/N lobe aromatic anchors uncovers their role in Ca(V)1.2 CDF. Together, our data suggest that Ca(V) subtype differences in CDI and CDF are tuned by changes in IQ domain anchoring positions and establish a framework for understanding CaM lobe-specific regulation of Ca(V)s.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16299511}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16299511 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16299511}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Iq domain]] | | [[Category: Iq domain]] |
| [[Category: Voltage-gated]] | | [[Category: Voltage-gated]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:10:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:34:17 2008'' |
