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protein metals Protein-protein interface(s) links
Signaling protein PDB id
1t0j
Jmol
Contents
Protein chains
96 a.a. *
187 a.a. *
16 a.a. *
Metals
_CL
Waters ×138
* Residue conservation analysis
PDB id:
1t0j
Name: Signaling protein
Title: Crystal structure of a complex between voltage-gated calcium beta2a subunit and a peptide of the alpha1c subunit
Structure: Voltage-gated calcium channel subunit beta2a. Chain: a. Fragment: residues 17-145. Engineered: yes. Voltage-gated calcium channel subunit beta2a. Chain: b. Fragment: residues 203-425. Engineered: yes. Voltage-dependent l-type calcium channel alpha-1c
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: cacnb2a. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.
Biol. unit: Trimer (from PQS)
Resolution:
2.00Å     R-factor:   0.202     R-free:   0.242
Authors: F.Van Petegem,K.Clark,F.Chatelain,D.Minor Jr.
Key ref:
F.Van Petegem et al. (2004). Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain. Nature, 429, 671-675. PubMed id: 15141227 DOI: 10.1038/nature02588
Date:
09-Apr-04     Release date:   15-Jun-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q8VGC3  (CACB2_RAT) -  Voltage-dependent L-type calcium channel subunit beta-2
Seq:
Struc: 		 
Seq:
Struc: 		655 a.a.
96 a.a.
Protein chain
Pfam   ArchSchema ?
Q8VGC3  (CACB2_RAT) -  Voltage-dependent L-type calcium channel subunit beta-2
Seq:
Struc: 		 
Seq:
Struc: 		655 a.a.
187 a.a.*
Protein chain
Pfam   ArchSchema ?
Q13936  (CAC1C_HUMAN) -  Voltage-dependent L-type calcium channel subunit alpha-1C
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		2221 a.a.
16 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     integral to membrane   1 term 
  Biological process     calcium ion transport   2 terms 
  Biochemical function     protein binding     2 terms  

 

 
DOI no: 10.1038/nature02588 Nature 429:671-675 (2004)
PubMed id: 15141227  
 
 
Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain.
F.Van Petegem, K.A.Clark, F.C.Chatelain, D.L.Minor.
 
  ABSTRACT  
 
Voltage-gated calcium channels (Ca(V)s) govern muscle contraction, hormone and neurotransmitter release, neuronal migration, activation of calcium-dependent signalling cascades, and synaptic input integration. An essential Ca(V) intracellular protein, the beta-subunit (Ca(V)beta), binds a conserved domain (the alpha-interaction domain, AID) between transmembrane domains I and II of the pore-forming alpha(1) subunit and profoundly affects multiple channel properties such as voltage-dependent activation, inactivation rates, G-protein modulation, drug sensitivity and cell surface expression. Here, we report the high-resolution crystal structures of the Ca(V)beta2a conserved core, alone and in complex with the AID. Previous work suggested that a conserved region, the beta-interaction domain (BID), formed the AID-binding site; however, this region is largely buried in the Ca(V)beta core and is unavailable for protein-protein interactions. The structure of the AID-Ca(V)beta2a complex shows instead that Ca(V)beta2a engages the AID through an extensive, conserved hydrophobic cleft (named the alpha-binding pocket, ABP). The ABP-AID interaction positions one end of the Ca(V)beta near the intracellular end of a pore-lining segment, called IS6, that has a critical role in Ca(V) inactivation. Together, these data suggest that Ca(V)betas influence Ca(V) gating by direct modulation of IS6 movement within the channel pore.
 
  Selected figure(s)  
 
Figure 2.
Figure 2: Structural comparisons between PSD-95 (gold) and Ca[V] beta-[2a] (blue). a, Superposition of Ca[V] [2a] and PSD-95 nucleotide kinase domains (RMSD[C ]= 3.9 Å). The dashed circle indicates the guanosine-monophosphate (GMP)-binding domain present in PSD-95 but absent in Ca[V] [2a]. The guanosine monophosphate molecule bound to PSD-95 is displayed in space-filling representation. Nucleotide kinase (NK) and SH3 domains are indicated. The relative change in SH3 domain orientation is indicated. b, Superposition of PSD-95 and Ca[V] [2a] SH3 domains (RMSD[C ]= 1.6 Å). Position of the polyproline ligand from a superposition with the Sem5 SH3 domain (Protein Data Bank code 2SEM) (RMSD[C ]= 1.8 Å) is shown in space-filling representation. The Sem5 SH3 is not shown. The DALI server generated the superpositions (http://www.ebi.ac.uk/dali/). 		Figure 4.
Figure 4: AID -ABP interactions. a, Surface representation of the Ca[V] [2a] ABP, bound to the AID. The AID (gold) is shown in stick representation. Y437 and W440 are white. Ca[V] [2a] residues that contribute hydrophobic (blue) and hydrogen bond (red) side-chain contacts to the AID are labelled. Select residues of the AID are labelled to orient the reader. b, c, Slices through the AID -ABP interaction at AID positions Y437 and W440 (gold). Labels indicate the AID residues.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (2004, 429, 671-675) copyright 2004.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21186355 C.Altier, A.Garcia-Caballero, B.Simms, H.You, L.Chen, J.Walcher, H.W.Tedford, T.Hermosilla, and G.W.Zamponi (2011).
The Cavβ subunit prevents RFP2-mediated ubiquitination and proteasomal degradation of L-type channels.
  Nat Neurosci, 14, 173-180.  
20451250 A.Dayal, J.Schredelseker, C.Franzini-Armstrong, and M.Grabner (2010).
Skeletal muscle excitation-contraction coupling is independent of a conserved heptad repeat motif in the C-terminus of the DHPRbeta(1a) subunit.
  Cell Calcium, 47, 500-506.  
21048710 C.C.Tung, P.A.Lobo, L.Kimlicka, and F.Van Petegem (2010).
The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule.
  Nature, 468, 585-588.
PDB code: 2xoa
21139419 D.L.Minor, and F.Findeisen (2010).
Progress in the structural understanding of voltage-gated calcium channel (CaV) function and modulation.
  Channels (Austin), 4, 459-474.  
20953164 E.Y.Kim, C.H.Rumpf, F.Van Petegem, R.J.Arant, F.Findeisen, E.S.Cooley, E.Y.Isacoff, and D.L.Minor (2010).
Multiple C-terminal tail Ca(2+)/CaMs regulate Ca(V)1.2 function but do not mediate channel dimerization.
  EMBO J, 29, 3924-3938.
PDB code: 3oxq
21134641 F.Findeisen, and D.L.Minor (2010).
Structural basis for the differential effects of CaBP1 and calmodulin on Ca(V)1.2 calcium-dependent inactivation.
  Structure, 18, 1617-1631.
PDB codes: 3ox5 3ox6
19996312 G.J.Obermair, B.Schlick, V.Di Biase, P.Subramanyam, M.Gebhart, S.Baumgartner, and B.E.Flucher (2010).
Reciprocal interactions regulate targeting of calcium channel beta subunits and membrane expression of alpha1 subunits in cultured hippocampal neurons.
  J Biol Chem, 285, 5776-5791.  
20181083 H.W.Tedford, A.E.Kisilevsky, L.B.Vieira, D.Varela, L.Chen, and G.W.Zamponi (2010).
Scanning mutagenesis of the I-II loop of the Cav2.2 calcium channel identifies residues Arginine 376 and Valine 416 as molecular determinants of voltage dependent G protein inhibition.
  Mol Brain, 3, 6.  
20803093 J.Bae, E.J.Suh, and C.Lee (2010).
Interaction of T-type calcium channel Ca(V)3.3 with the β-subunit.
  Mol Cells, 30, 185-191.  
  20584887 K.G.Beam, and R.A.Bannister (2010).
Looking for answers to EC coupling's persistent questions.
  J Gen Physiol, 136, 7.  
19995890 K.Murata, S.Nishimura, A.Kuniyasu, and H.Nakayama (2010).
Three-dimensional structure of the alpha1-beta complex in the skeletal muscle dihydropyridine receptor by single-particle electron microscopy.
  J Electron Microsc (Tokyo), 59, 215-226.  
  20142517 M.R.Tadross, M.Ben Johny, and D.T.Yue (2010).
Molecular endpoints of Ca2+/calmodulin- and voltage-dependent inactivation of Ca(v)1.3 channels.
  J Gen Physiol, 135, 197-215.  
19840220 S.A.Abiria, and R.J.Colbran (2010).
CaMKII associates with CaV1.2 L-type calcium channels via selected beta subunits to enhance regulatory phosphorylation.
  J Neurochem, 112, 150-161.  
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Inactivation of L-type calcium channels is determined by the length of the N terminus of mutant beta(1) subunits.
  Pflugers Arch, 459, 399-411.  
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The beta subunit of voltage-gated Ca2+ channels interacts with and regulates the activity of a novel isoform of Pax6.
  J Biol Chem, 285, 2527-2536.  
18651169 A.V.Dresviannikov, K.M.Page, J.Leroy, W.S.Pratt, and A.C.Dolphin (2009).
Determinants of the voltage dependence of G protein modulation within calcium channel beta subunits.
  Pflugers Arch, 457, 743-756.  
19492014 E.Kobrinsky, P.Abrahimi, S.Q.Duong, S.Thomas, J.B.Harry, C.Patel, Q.Z.Lao, and N.M.Soldatov (2009).
Effect of Ca(v)beta subunits on structural organization of Ca(v)1.2 calcium channels.
  PLoS One, 4, e5587.  
  19237593 F.Findeisen, and D.L.Minor (2009).
Disruption of the IS6-AID linker affects voltage-gated calcium channel inactivation and facilitation.
  J Gen Physiol, 133, 327-343.  
  19858356 J.Striessnig (2009).
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  J Gen Physiol, 134, 363-367.  
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  Structure, 17, 1505-1514.
PDB codes: 3ila 3im5 3im6 3im7
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  Hum Mutat, 30, 1256-1266.  
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  Hum Mutat, 30, 1486-1511.  
  19755859 P.Subramanyam, G.J.Obermair, S.Baumgartner, M.Gebhart, J.Striessnig, W.A.Kaufmann, S.Geley, and B.E.Flucher (2009).
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  Channels (Austin), 3, 343-355.  
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  Protein Sci, 18, 2100-2114.
PDB codes: 3hfc 3hfe
  19342611 S.Dai, D.D.Hall, and J.W.Hell (2009).
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  Physiol Rev, 89, 411-452.  
  19858358 T.Mitra-Ganguli, I.Vitko, E.Perez-Reyes, and A.R.Rittenhouse (2009).
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  J Gen Physiol, 134, 385-396.  
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  Nat Rev Neurosci, 10, 87-99.  
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  Physiology (Bethesda), 24, 210-218.  
19427861 Y.H.Chen, L.L.He, D.R.Buchanan, Y.Zhang, A.Fitzmaurice, and J.Yang (2009).
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  FEBS Lett, 583, 1969-1975.  
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  Proc Natl Acad Sci U S A, 105, 198-203.  
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  BMC Mol Biol, 9, 38.  
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Genomic organization, expression, and phylogenetic analysis of Ca2+ channel beta4 genes in 13 vertebrate species.
  Physiol Genomics, 35, 133-144.  
18535142 A.Ravindran, Q.Z.Lao, J.B.Harry, P.Abrahimi, E.Kobrinsky, and N.M.Soldatov (2008).
Calmodulin-dependent gating of Ca(v)1.2 calcium channels in the absence of Ca(v)beta subunits.
  Proc Natl Acad Sci U S A, 105, 8154-8159.  
17929154 A.Y.Kuznetsova, and R.C.Deth (2008).
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  J Comput Neurosci, 24, 314-329.  
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Differential regulated interactions of calcium/calmodulin-dependent protein kinase II with isoforms of voltage-gated calcium channel beta subunits.
  Biochemistry, 47, 1760-1767.  
18339621 D.Jeon, I.Song, W.Guido, K.Kim, E.Kim, U.Oh, and H.S.Shin (2008).
Ablation of Ca2+ channel beta3 subunit leads to enhanced N-methyl-D-aspartate receptor-dependent long term potentiation and improved long term memory.
  J Biol Chem, 283, 12093-12101.  
18940602 E.Y.Kim, C.H.Rumpf, Y.Fujiwara, E.S.Cooley, F.Van Petegem, and D.L.Minor (2008).
Structures of CaV2 Ca2+/CaM-IQ domain complexes reveal binding modes that underlie calcium-dependent inactivation and facilitation.
  Structure, 16, 1455-1467.
PDB codes: 3dve 3dvj 3dvk 3dvm
18275819 F.Van Petegem, K.E.Duderstadt, K.A.Clark, M.Wang, and D.L.Minor (2008).
Alanine-scanning mutagenesis defines a conserved energetic hotspot in the CaValpha1 AID-CaVbeta interaction site that is critical for channel modulation.
  Structure, 16, 280-294.  
  18725532 G.Gonzalez-Gutierrez, E.Miranda-Laferte, D.Naranjo, P.Hidalgo, and A.Neely (2008).
Mutations of nonconserved residues within the calcium channel alpha1-interaction domain inhibit beta-subunit potentiation.
  J Gen Physiol, 132, 383-395.  
18776052 G.Gonzalez-Gutierrez, E.Miranda-Laferte, D.Nothmann, S.Schmidt, A.Neely, and P.Hidalgo (2008).
The guanylate kinase domain of the beta-subunit of voltage-gated calcium channels suffices to modulate gating.
  Proc Natl Acad Sci U S A, 105, 14198-14203.  
18958281 I.Vitko, A.Shcheglovitov, J.P.Baumgart, I.I.Arias-Olguín, J.Murbartián, J.M.Arias, and E.Perez-Reyes (2008).
Orientation of the calcium channel beta relative to the alpha(1)2.2 subunit is critical for its regulation of channel activity.
  PLoS ONE, 3, e3560.  
18509027 K.Yu, Q.Xiao, G.Cui, A.Lee, and H.C.Hartzell (2008).
The best disease-linked Cl- channel hBest1 regulates Ca V 1 (L-type) Ca2+ channels via src-homology-binding domains.
  J Neurosci, 28, 5660-5670.  
18628210 M.Murakami, T.Ohba, F.Xu, E.Satoh, I.Miyoshi, T.Suzuki, Y.Takahashi, E.Takahashi, H.Watanabe, K.Ono, H.Sasano, N.Kasai, H.Ito, and T.Iijima (2008).
Modified Sympathetic Nerve System Activity with Overexpression of the Voltage-dependent Calcium Channel {beta}3 Subunit.
  J Biol Chem, 283, 24554-24560.  
18411278 Q.Z.Lao, E.Kobrinsky, J.B.Harry, A.Ravindran, and N.M.Soldatov (2008).
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  J Biol Chem, 283, 15577-15588.  
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The RGK family of GTP-binding proteins: regulators of voltage-dependent calcium channels and cytoskeleton remodeling.
  Cell Signal, 20, 292-300.  
18068949 R.N.Correll, G.J.Botzet, J.Satin, D.A.Andres, and B.S.Finlin (2008).
Analysis of the Rem2 - voltage dependant calcium channel beta subunit interaction and Rem2 interaction with phosphorylated phosphatidylinositide lipids.
  Cell Signal, 20, 400-408.  
18782578 Y.Fujiwara, and D.L.Minor (2008).
X-ray crystal structure of a TRPM assembly domain reveals an antiparallel four-stranded coiled-coil.
  J Mol Biol, 383, 854-870.
PDB code: 3e7k
19109500 Y.Zhang, Y.H.Chen, S.D.Bangaru, L.He, K.Abele, S.Tanabe, T.Kozasa, and J.Yang (2008).
Origin of the voltage dependence of G-protein regulation of P/Q-type Ca2+ channels.
  J Neurosci, 28, 14176-14188.  
17521566 D.L.Minor (2007).
The neurobiologist's guide to structural biology: a primer on why macromolecular structure matters and how to evaluate structural data.
  Neuron, 54, 511-533.  
17110381 G.Gonzalez-Gutierrez, E.Miranda-Laferte, A.Neely, and P.Hidalgo (2007).
The Src homology 3 domain of the beta-subunit of voltage-gated calcium channels promotes endocytosis via dynamin interaction.
  J Biol Chem, 282, 2156-2162.  
18001290 K.S.Richards, A.M.Swensen, D.Lipscombe, and K.Bommert (2007).
Novel CaV2.1 clone replicates many properties of Purkinje cell CaV2.1 current.
  Eur J Neurosci, 26, 2950-2961.  
17496037 L.L.He, Y.Zhang, Y.H.Chen, Y.Yamada, and J.Yang (2007).
Functional modularity of the beta-subunit of voltage-gated Ca2+ channels.
  Biophys J, 93, 834-845.  
17220895 M.L.Reese, S.Dakoji, D.S.Bredt, and V.Dötsch (2007).
The guanylate kinase domain of the MAGUK PSD-95 binds dynamically to a conserved motif in MAP1a.
  Nat Struct Mol Biol, 14, 155-163.  
17664337 M.Xie, X.Li, J.Han, D.L.Vogt, S.Wittemann, M.D.Mark, and S.Herlitze (2007).
Facilitation versus depression in cultured hippocampal neurons determined by targeting of Ca2+ channel Cavbeta4 versus Cavbeta2 subunits to synaptic terminals.
  J Cell Biol, 178, 489-502.  
17303572 P.Béguin, Y.J.Ng, C.Krause, R.N.Mahalakshmi, M.Y.Ng, and W.Hunziker (2007).
RGK small GTP-binding proteins interact with the nucleotide kinase domain of Ca2+-channel beta-subunits via an uncommon effector binding domain.
  J Biol Chem, 282, 11509-11520.  
17899404 R.A.Bannister (2007).
Bridging the myoplasmic gap: recent developments in skeletal muscle excitation-contraction coupling.
  J Muscle Res Cell Motil, 28, 275-283.  
17329207 R.J.Howard, K.A.Clark, J.M.Holton, and D.L.Minor (2007).
Structural insight into KCNQ (Kv7) channel assembly and channelopathy.
  Neuron, 53, 663-675.
PDB code: 2ovc
17526524 Y.L.Lai, S.C.Yen, S.H.Yu, and J.K.Hwang (2007).
pKNOT: the protein KNOT web server.
  Nucleic Acids Res, 35, W420-W424.  
17028169 A.Badou, M.K.Jha, D.Matza, W.Z.Mehal, M.Freichel, V.Flockerzi, and R.A.Flavell (2006).
Critical role for the beta regulatory subunits of Cav channels in T lymphocyte function.
  Proc Natl Acad Sci U S A, 103, 15529-15534.  
16402121 A.C.Dolphin (2006).
A short history of voltage-gated calcium channels.
  Br J Pharmacol, 147, S56-S62.  
16385006 A.C.Vendel, C.D.Rithner, B.A.Lyons, and W.A.Horne (2006).
Solution structure of the N-terminal A domain of the human voltage-gated Ca2+channel beta4a subunit.
  Protein Sci, 15, 378-383.
PDB code: 2d46
16627564 A.J.Butcher, J.Leroy, M.W.Richards, W.S.Pratt, and A.C.Dolphin (2006).
The importance of occupancy rather than affinity of CaV(beta) subunits for the calcium channel I-II linker in relation to calcium channel function.
  J Physiol, 574, 387-398.  
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Two PEST-like motifs regulate Ca2+/calpain-mediated cleavage of the CaVbeta3 subunit and provide important determinants for neuronal Ca2+ channel activity.
  Eur J Neurosci, 23, 2311-2320.  
16790445 B.S.Finlin, R.N.Correll, C.Pang, S.M.Crump, J.Satin, and D.A.Andres (2006).
Analysis of the complex between Ca2+ channel beta-subunit and the Rem GTPase.
  J Biol Chem, 281, 23557-23566.  
16949361 C.E.Grueter, S.A.Abiria, I.Dzhura, Y.Wu, A.J.Ham, P.J.Mohler, M.E.Anderson, and R.J.Colbran (2006).
L-type Ca2+ channel facilitation mediated by phosphorylation of the beta subunit by CaMKII.
  Mol Cell, 23, 641-650.  
  17052221 F.Van Petegem, and D.L.Minor (2006).
The structural biology of voltage-gated calcium channel function and regulation.
  Biochem Soc Trans, 34, 887-893.  
  17074979 L.Seu, and G.S.Pitt (2006).
Dose-dependent and isoform-specific modulation of Ca2+ channels by RGK GTPases.
  J Gen Physiol, 128, 605-613.  
17057713 M.Pioletti, F.Findeisen, G.L.Hura, and D.L.Minor (2006).
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer.
  Nat Struct Mol Biol, 13, 987-995.
PDB code: 2i2r
  16801381 N.Kanevsky, and N.Dascal (2006).
Regulation of maximal open probability is a separable function of Ca(v)beta subunit in L-type Ca2+ channel, dependent on NH2 terminus of alpha1C (Ca(v)1.2alpha).
  J Gen Physiol, 128, 15-36.  
16846855 P.R.Tsuruda, D.Julius, and D.L.Minor (2006).
Coiled coils direct assembly of a cold-activated TRP channel.
  Neuron, 51, 201-212.  
16942804 R.M.Evans, and G.W.Zamponi (2006).
Presynaptic Ca2+ channels--integration centers for neuronal signaling pathways.
  Trends Neurosci, 29, 617-624.  
16317008 V.Leuranguer, S.Papadopoulos, and K.G.Beam (2006).
Organization of calcium channel beta1a subunits in triad junctions in skeletal muscle.
  J Biol Chem, 281, 3521-3527.  
16157588 A.Hohaus, S.Beyl, M.Kudrnac, S.Berjukow, E.N.Timin, R.Marksteiner, M.A.Maw, and S.Hering (2005).
Structural determinants of L-type channel activation in segment IIS6 revealed by a retinal disorder.
  J Biol Chem, 280, 38471-38477.  
16088377 B.E.Flucher, G.J.Obermair, P.Tuluc, J.Schredelseker, G.Kern, and M.Grabner (2005).
The role of auxiliary dihydropyridine receptor subunits in muscle.
  J Muscle Res Cell Motil, 26, 1-6.  
16299511 F.Van Petegem, F.C.Chatelain, and D.L.Minor (2005).
Insights into voltage-gated calcium channel regulation from the structure of the CaV1.2 IQ domain-Ca2+/calmodulin complex.
  Nat Struct Mol Biol, 12, 1108-1115.
PDB code: 2be6
15953418 H.L.Agler, J.Evans, L.H.Tay, M.J.Anderson, H.M.Colecraft, and D.T.Yue (2005).
G protein-gated inhibitory module of N-type (ca(v)2.2) ca2+ channels.
  Neuron, 46, 891-904.  
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The L-type calcium channel in the heart: the beat goes on.
  J Clin Invest, 115, 3306-3317.  
15750602 J.M.Maltez, D.A.Nunziato, J.Kim, and G.S.Pitt (2005).
Essential Ca(V)beta modulatory properties are AID-independent.
  Nat Struct Mol Biol, 12, 372-377.  
16286639 J.Schredelseker, V.Di Biase, G.J.Obermair, E.T.Felder, B.E.Flucher, C.Franzini-Armstrong, and M.Grabner (2005).
The beta 1a subunit is essential for the assembly of dihydropyridine-receptor arrays in skeletal muscle.
  Proc Natl Acad Sci U S A, 102, 17219-17224.  
15507442 L.Berrou, Y.Dodier, A.Raybaud, A.Tousignant, O.Dafi, J.N.Pelletier, and L.Parent (2005).
The C-terminal residues in the alpha-interacting domain (AID) helix anchor CaV beta subunit interaction and modulation of CaV2.3 channels.
  J Biol Chem, 280, 494-505.  
15952887 L.Funke, S.Dakoji, and D.S.Bredt (2005).
Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions.
  Annu Rev Biochem, 74, 219-245.  
16009433 M.De Waard, J.Hering, N.Weiss, and A.Feltz (2005).
How do G proteins directly control neuronal Ca2+ channel function?
  Trends Pharmacol Sci, 26, 427-436.  
15816172 R.J.French, and G.W.Zamponi (2005).
Voltage-gated sodium and calcium channels in nerve, muscle, and heart.
  IEEE Trans Nanobioscience, 4, 58-69.  
  16569296 R.M.Greenberg (2005).
Ca2+ signalling, voltage-gated Ca2+ channels and praziquantel in flatworm neuromusculature.
  Parasitology, 131, S97-108.  
16020456 S.Dalton, S.X.Takahashi, J.Miriyala, and H.M.Colecraft (2005).
A single CaVbeta can reconstitute both trafficking and macroscopic conductance of voltage-dependent calcium channels.
  J Physiol, 567, 757-769.  
  16186563 S.X.Takahashi, J.Miriyala, L.H.Tay, D.T.Yue, and H.M.Colecraft (2005).
A CaVbeta SH3/guanylate kinase domain interaction regulates multiple properties of voltage-gated Ca2+ channels.
  J Gen Physiol, 126, 365-377.  
16357209 W.Cheng, X.Altafaj, M.Ronjat, and R.Coronado (2005).
Interaction between the dihydropyridine receptor Ca2+ channel beta-subunit and ryanodine receptor type 1 strengthens excitation-contraction coupling.
  Proc Natl Acad Sci U S A, 102, 19225-19230.  
15627376 I.I.Serysheva (2004).
Structural insights into excitation-contraction coupling by electron cryomicroscopy.
  Biochemistry (Mosc), 69, 1226-1232.  
15339916 J.B.Harry, E.Kobrinsky, D.R.Abernethy, and N.M.Soldatov (2004).
New short splice variants of the human cardiac Cavbeta2 subunit: redefining the major functional motifs implemented in modulation of the Cav1.2 channel.
  J Biol Chem, 279, 46367-46372.  
15265869 J.D.Spafford, J.Van Minnen, P.Larsen, A.B.Smit, N.I.Syed, and G.W.Zamponi (2004).
Uncoupling of calcium channel alpha1 and beta subunits in developing neurons.
  J Biol Chem, 279, 41157-41167.  
15530640 M.W.Richards, A.J.Butcher, and A.C.Dolphin (2004).
Ca2+ channel beta-subunits: structural insights AID our understanding.
  Trends Pharmacol Sci, 25, 626-632.  
15339810 O.Dafi, L.Berrou, Y.Dodier, A.Raybaud, R.Sauvé, and L.Parent (2004).
Negatively charged residues in the N-terminal of the AID helix confer slow voltage dependent inactivation gating to CaV1.2.
  Biophys J, 87, 3181-3192.  
15479643 P.O.Berggren, S.N.Yang, M.Murakami, A.M.Efanov, S.Uhles, M.Köhler, T.Moede, A.Fernström, I.B.Appelskog, C.A.Aspinwall, S.V.Zaitsev, O.Larsson, L.M.de Vargas, C.Fecher-Trost, P.Weissgerber, A.Ludwig, B.Leibiger, L.Juntti-Berggren, C.J.Barker, J.Gromada, M.Freichel, I.B.Leibiger, and V.Flockerzi (2004).
Removal of Ca2+ channel beta3 subunit enhances Ca2+ oscillation frequency and insulin exocytosis.
  Cell, 119, 273-284.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.