カルモジュリン結合ドメイン
WordNet
- executed with proper legal authority; "a binding contract"
- the protective covering on the front, back, and spine of a book; "the book had a leather binding" (同)book binding, cover, back
- strip sewn over or along an edge for reinforcement or decoration
- the capacity to attract and hold something
- territory over which rule or control is exercised; "his domain extended into Europe"; "he made it the law of the land" (同)demesne, land
- (mathematics) the set of values of the independent variable for which a function is defined (同)domain of a function
PrepTutorEJDIC
- 義務的な,拘束力ある / 〈U〉しばること;〈C〉しばる物 / 〈C〉製本,装丁 / 〈U〉縁(‘ふち')取り材料
- (国の)領地,領土;(個人の)所有地 / (関心・活動などの)範囲,分野 / (個人・一族の)所有地 / (数学で)変域(関数の独立変数がとる値の集合)
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2017/08/26 05:59:02」(JST)
[Wiki en表示]
CaMBD |
solution structure of the calmodulin binding domain (cambd) of small conductanceCa2+-activated potassium channels (sk2)
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Identifiers |
Symbol |
CaMBD |
Pfam |
PF02888 |
InterPro |
IPR004178 |
SCOP |
1kkd |
SUPERFAMILY |
1kkd |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
|
In molecular biology, calmodulin binding domain (CaMBD) is a protein domain found in small-conductance calcium-activated potassium channels (SK channels). These channels are independent of voltage and gated solely by intracellular Ca2+. They are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM).[1] CaM binds to the SK channel through the 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. The structure of this domain complexed with CaM is known.[1] This domain 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.
References
- ^ a b Schumacher MA, Rivard AF, Bachinger HP, Adelman JP (April 2001). "Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin". Nature. 410 (6832): 1120–4. PMID 11323678. doi:10.1038/35074145.
This article incorporates text from the public domain Pfam and InterPro IPR004178
UpToDate Contents
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English Journal
- Multiple domains in the C-terminus of NMDA receptor GluN2B subunit contribute to neuronal death following in vitro ischemia.
- Vieira MM1, Schmidt J2, Ferreira JS1, She K3, Oku S3, Mele M1, Santos AE4, Duarte CB5, Craig AM3, Carvalho AL6.
- Neurobiology of disease.Neurobiol Dis.2016 May;89:223-34. doi: 10.1016/j.nbd.2015.11.007. Epub 2015 Nov 12.
- Global cerebral ischemia induces selective degeneration of specific subsets of neurons throughout the brain, particularly in the hippocampus and cortex. One of the major hallmarks of cerebral ischemia is excitotoxicity, characterized by overactivation of glutamate receptors leading to intracellular
- PMID 26581639
- Fcγ1 fragment of IgG1 as a powerful affinity tag in recombinant Fc-fusion proteins: immunological, biochemical and therapeutic properties.
- Soleimanpour S1, Hassannia T2, Motiee M3, Amini AA4, Rezaee SA3.
- Critical reviews in biotechnology.Crit Rev Biotechnol.2016 Apr 6:1-22. [Epub ahead of print]
- Affinity tags are vital tools for the production of high-throughput recombinant proteins. Several affinity tags, such as the hexahistidine tag, maltose-binding protein, streptavidin-binding peptide tag, calmodulin-binding peptide, c-Myc tag, glutathione S-transferase and FLAG tag, have been introduc
- PMID 27049690
- Conformational heterogeneity of the calmodulin binding interface.
- Shukla D1,2,3, Peck A4, Pande VS1,2.
- Nature communications.Nat Commun.2016 Apr 4;7:10910. doi: 10.1038/ncomms10910.
- Calmodulin (CaM) is a ubiquitous Ca(2+) sensor and a crucial signalling hub in many pathways aberrantly activated in disease. However, the mechanistic basis of its ability to bind diverse signalling molecules including G-protein-coupled receptors, ion channels and kinases remains poorly understood.
- PMID 27040077
Japanese Journal
- Strong Interaction of Bovine Brain Calmodulin with Bisphenol A : Effects on Secondary Structure, Conformation, Ca²⁺-Binding Affinity, Gibbs Energy, and Domain Cooperativity
- Murayama Koichi,Sonoyama Masashi,Matsuda Sadayuki
- Bulletin of the Chemical Society of Japan 88(6), 880-887, 2015
- … Calmodulin (CaM) is a major member of the family of Ca2+-binding proteins. … In this study, effects on Ca2+-binding affinity and conformation of CaM by bisphenol A (BPA) were investigated by using circular dichroism and UV absorbance spectroscopy, domain-specific fluorescence spectroscopy, and isothermal titration calorimetry. …
- NAID 130005075687
- Negatively Charged Amino Acids Near and in Transient Receptor Potential (TRP) Domain of TRPM4 Channel Are One Determinant of Its Ca2+ Sensitivity.
- Yamaguchi Soichiro,Tanimoto Akira,Otsuguro Ken-ichi,Hibino Hiroshi,Ito Shigeo
- The Journal of biological chemistry 289(51), 35265-35282, 2014-12-19
- … The Ca2+ sensitivity is known to be regulated by calmodulin and membrane phosphoinositides, such as phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). … Although these regulators must play important roles in controlling TRPM4 activity, mutation analyses of the calmodulin-binding sites have suggested that Ca2+ binds to TRPM4 directly. … However, the intrinsic binding sites in TRPM4 remain to be elucidated. …
- NAID 120005522343
- Ran and Calcineurin Can Participate Collaboratively in the Regulation of Spermatogenesis in Scallop
- Hino Hirotsugu,Arimoto Kana,Yazawa Michio,Murakami Yota,Nakatomi Akiko
- Marine Biotechnology 14(4), 479-490, 2012-08
- … Calcineurin is a calcium/calmodulin-dependent protein phosphatase that plays important roles in the transduction of calcium signals in a variety of tissues. … A novel calcineurin-binding protein, CaNBP75, has been identified in scallop testis. … The C-terminal region of CaNBP75 is homologous to the C-terminal region of RanBP3, a Ran binding domain-containing protein. …
- NAID 120004593470
Related Links
- Solution structure of the calmodulin binding domain (cambd) of small conductance ca2+-activated potassium channels (sk2) 1qx7 Crystal structure of apocam bound to the gating domain of small conductance ca2+-activated Links ...
- Calmodulin Binding Domain September 8, 2011 – 10:30 am Because healthy proteins is important so that you can life-style, all of life-forms contains aminoacids; however, the specified healthy proteins material changes. Usually » ...
★リンクテーブル★
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- 英
- calmodulin binding domain
- 同
- CaM結合ドメイン
- 関
- カルモジュリン
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- 関
- affinity、associate、bind、bond、bonding、combine、conjoin、conjugate、conjugation、conjunction、connect、connection、connective、connectivity、couple、dock、engage、engagement、join、ligate、linkage、symphysial、symphysic、union
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- 関
- area、realm、region、regional、segregation、territory、universe
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カルモジュリン CaM
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- 関
- See also specific type