1qx7
From Proteopedia
(New page: 200px<br /><applet load="1qx7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qx7, resolution 3.09Å" /> '''Crystal structure of...) |
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| - | [[Image:1qx7.gif|left|200px]]<br /><applet load="1qx7" size=" | + | [[Image:1qx7.gif|left|200px]]<br /><applet load="1qx7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qx7, resolution 3.09Å" /> | caption="1qx7, resolution 3.09Å" /> | ||
'''Crystal structure of apoCaM bound to the gating domain of small conductance Ca2+-activated potassium channel'''<br /> | '''Crystal structure of apoCaM bound to the gating domain of small conductance Ca2+-activated potassium channel'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Small conductance Ca2+-activated K+ channels (SK channels) are composed of | + | Small conductance Ca2+-activated K+ channels (SK channels) are composed of the pore-forming alpha subunit and calmodulin (CaM). CaM binds to a region of the alpha subunit called the CaM binding domain (CaMBD), located intracellular and immediately C-terminal to the inner helix gate, in either the presence or absence of Ca2+. SK gating occurs when Ca2+ binds the N lobe of CaM thereby transmitting the signal to the attached inner helix gate to open. Here we present crystal structures of apoCaM and apoCaM/SK2 CaMBD complex. Several apoCaM crystal forms with multiple (12) packing environments reveal the same EF hand domain-swapped dimer providing potentially new insight into CaM regulation. The apoCaM/SK2 CaMBD structure, combined with our Ca2+/CaM/CaMBD structure suggests that Ca2+ binding induces folding and dimerization of the CaMBD, which causes large CaMBD-CaM C lobe conformational changes, including a >90 degrees rotation of the region of the CaMBD directly connected to the gate. |
==About this Structure== | ==About this Structure== | ||
| - | 1QX7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1QX7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QX7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Crum, M.]] | [[Category: Crum, M.]] | ||
| - | [[Category: Miller, M | + | [[Category: Miller, M C.]] |
| - | [[Category: Schumacher, M | + | [[Category: Schumacher, M A.]] |
[[Category: apocalmodulin]] | [[Category: apocalmodulin]] | ||
[[Category: ca2+-activated gating]] | [[Category: ca2+-activated gating]] | ||
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[[Category: small conductance ca2+ activated k+ channel]] | [[Category: small conductance ca2+ activated k+ channel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:42 2008'' |
Revision as of 12:44, 21 February 2008
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Crystal structure of apoCaM bound to the gating domain of small conductance Ca2+-activated potassium channel
Overview
Small conductance Ca2+-activated K+ channels (SK channels) are composed of the pore-forming alpha subunit and calmodulin (CaM). CaM binds to a region of the alpha subunit called the CaM binding domain (CaMBD), located intracellular and immediately C-terminal to the inner helix gate, in either the presence or absence of Ca2+. SK gating occurs when Ca2+ binds the N lobe of CaM thereby transmitting the signal to the attached inner helix gate to open. Here we present crystal structures of apoCaM and apoCaM/SK2 CaMBD complex. Several apoCaM crystal forms with multiple (12) packing environments reveal the same EF hand domain-swapped dimer providing potentially new insight into CaM regulation. The apoCaM/SK2 CaMBD structure, combined with our Ca2+/CaM/CaMBD structure suggests that Ca2+ binding induces folding and dimerization of the CaMBD, which causes large CaMBD-CaM C lobe conformational changes, including a >90 degrees rotation of the region of the CaMBD directly connected to the gate.
About this Structure
1QX7 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex., Schumacher MA, Crum M, Miller MC, Structure. 2004 May;12(5):849-60. PMID:15130477
Page seeded by OCA on Thu Feb 21 14:44:42 2008
