RGD Reference Report - Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex. - Rat Genome Database

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Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex.

Authors: Schumacher, MA  Crum, M  Miller, MC 
Citation: Schumacher MA, etal., Structure. 2004 May;12(5):849-60.
RGD ID: 8554118
Pubmed: PMID:15130477   (View Abstract at PubMed)
DOI: DOI:10.1016/j.str.2004.03.017   (Journal Full-text)

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.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
protein binding enablesIPIUniProtKB:P706048554118; 8554118; 8554118PMID:15130477IntAct 
protein binding enablesIPIUniProtKB:P0DP298554118PMID:15130477IntAct 

Objects Annotated

Genes (Rattus norvegicus)
Calm1  (calmodulin 1)
Calm2  (calmodulin 2)
Calm3  (calmodulin 3)
Kcnn2  (potassium calcium-activated channel subfamily N member 2)


Additional Information