1g4y

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(New page: 200px<br /><applet load="1g4y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g4y, resolution 1.60&Aring;" /> '''1.60 A CRYSTAL STRUC...)
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'''1.60 A CRYSTAL STRUCTURE OF THE GATING DOMAIN FROM SMALL CONDUCTANCE POTASSIUM CHANNEL COMPLEXED WITH CALCIUM-CALMODULIN'''<br />
'''1.60 A CRYSTAL STRUCTURE OF THE GATING DOMAIN FROM SMALL CONDUCTANCE POTASSIUM CHANNEL COMPLEXED WITH CALCIUM-CALMODULIN'''<br />
==Overview==
==Overview==
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Small-conductance Ca2+-activated K+ channels (SK channels) are independent, of voltage and gated solely by intracellular Ca2+. These membrane channels, are heteromeric complexes that comprise pore-forming alpha-subunits and, the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel, through the CaM-binding domain (CaMBD), which is located in an, intracellular region of the alpha-subunit immediately carboxy-terminal to, the pore. Channel opening is triggered when Ca2+ binds the EF hands in the, N-lobe of CaM. Here we report the 1.60 A crystal structure of the SK, channel CaMBD/Ca2+/CaM complex. The CaMBD forms an elongated dimer with a, CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. As only the CaM N-lobe, has bound Ca2+, the structure provides a view of both calcium-dependent, and -independent CaM/protein interactions. Together with biochemical data, the structure suggests a possible gating mechanism for the SK channel.
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Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. Here we report the 1.60 A crystal structure of the SK channel CaMBD/Ca2+/CaM complex. The CaMBD forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. As only the CaM N-lobe has bound Ca2+, the structure provides a view of both calcium-dependent and -independent CaM/protein interactions. Together with biochemical data, the structure suggests a possible gating mechanism for the SK channel.
==About this Structure==
==About this Structure==
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1G4Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G4Y OCA].
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1G4Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G4Y OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Adelman, J.P.]]
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[[Category: Adelman, J P.]]
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[[Category: Bachinger, H.P.]]
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[[Category: Bachinger, H P.]]
[[Category: Rivard, A.]]
[[Category: Rivard, A.]]
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[[Category: Schumacher, M.A.]]
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[[Category: Schumacher, M A.]]
[[Category: CA]]
[[Category: CA]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: small-conductance calcium-activated potassium channel]]
[[Category: small-conductance calcium-activated potassium channel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:42:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:07 2008''

Revision as of 10:46, 21 February 2008


1g4y, resolution 1.60Å

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1.60 A CRYSTAL STRUCTURE OF THE GATING DOMAIN FROM SMALL CONDUCTANCE POTASSIUM CHANNEL COMPLEXED WITH CALCIUM-CALMODULIN

Overview

Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. Here we report the 1.60 A crystal structure of the SK channel CaMBD/Ca2+/CaM complex. The CaMBD forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. As only the CaM N-lobe has bound Ca2+, the structure provides a view of both calcium-dependent and -independent CaM/protein interactions. Together with biochemical data, the structure suggests a possible gating mechanism for the SK channel.

About this Structure

1G4Y is a Protein complex structure of sequences from Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin., Schumacher MA, Rivard AF, Bachinger HP, Adelman JP, Nature. 2001 Apr 26;410(6832):1120-4. PMID:11323678

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