SASDAN4: Calmodulin:peptide complex (Calmodulin + C-terminal region of hum...

基本情報

• 登録情報: データベース: SASBDB / ID: SASDAN4

試料

Calmodulin:peptide complex

• Calmodulin (protein), Homo sapiens
• C-terminal region of human myelin basic protein (protein), peptide, Homo sapiens

機能・相同性

分子機能:

: / : / positive regulation of cyclic-nucleotide phosphodiesterase activity / : / establishment of protein localization to mitochondrial membrane / negative regulation of peptidyl-threonine phosphorylation / type 3 metabotropic glutamate receptor binding / positive regulation of DNA binding / negative regulation of high voltage-gated calcium channel activity / response to corticosterone / positive regulation of peptidyl-threonine phosphorylation / nitric-oxide synthase binding / negative regulation of calcium ion export across plasma membrane / regulation of synaptic vesicle exocytosis / regulation of cardiac muscle cell action potential / positive regulation of ryanodine-sensitive calcium-release channel activity / regulation of cell communication by electrical coupling involved in cardiac conduction / negative regulation of ryanodine-sensitive calcium-release channel activity / regulation of synaptic vesicle endocytosis / positive regulation of protein autophosphorylation / protein phosphatase activator activity / adenylate cyclase binding / catalytic complex / detection of calcium ion / regulation of cardiac muscle contraction / positive regulation of protein serine/threonine kinase activity / phosphatidylinositol 3-kinase binding / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / activation of adenylate cyclase activity / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / enzyme regulator activity / regulation of calcium-mediated signaling / titin binding / voltage-gated potassium channel complex / substantia nigra development / calcium channel complex / nitric-oxide synthase regulator activity / response to amphetamine / positive regulation of nitric-oxide synthase activity / adenylate cyclase activator activity / regulation of heart rate / protein serine/threonine kinase activator activity / sarcomere / regulation of cytokinesis / spindle microtubule / mitochondrial membrane / response to calcium ion / synaptic vesicle membrane / spindle pole / calcium-dependent protein binding / G2/M transition of mitotic cell cycle / disordered domain specific binding / myelin sheath / growth cone / vesicle / transmembrane transporter binding / G protein-coupled receptor signaling pathway / protein domain specific binding / centrosome / calcium ion binding / protein kinase binding / protein-containing complex / nucleus / plasma membrane / cytoplasm

ドメイン・相同性:

EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair

構成要素:

Calmodulin-3

• 生物種: Homo sapiens (ヒト)
• 引用: ジャーナル: BMC Struct Biol / 年: 2008; タイトル: Interaction between the C-terminal region of human myelin basic protein and calmodulin: analysis of complex formation and solution structure.; 著者: Viivi Majava / Maxim V Petoukhov / Nobuhiro Hayashi / Päivi Pirilä / Dmitri I Svergun / Petri Kursula / ; 要旨: BACKGROUND: The myelin sheath is a multilamellar membrane structure wrapped around the axon, enabling the saltatory conduction of nerve impulses in vertebrates. Myelin basic protein, one of the most abundant myelin-specific proteins, is an intrinsically disordered protein that has been shown to bind calmodulin. In this study, we focus on a 19-mer synthetic peptide from the predicted calmodulin-binding segment near the C-terminus of human myelin basic protein.; RESULTS: The interaction of native human myelin basic protein with calmodulin was confirmed by affinity chromatography. The binding of the myelin basic protein peptide to calmodulin was tested with isothermal titration calorimetry (ITC) in different temperatures, and Kd was observed to be in the low muM range, as previously observed for full-length myelin basic protein. Surface plasmon resonance showed that the peptide bound to calmodulin, and binding was accompanied by a conformational change; furthermore, gel filtration chromatography indicated a decrease in the hydrodynamic radius of calmodulin in the presence of the peptide. NMR spectroscopy was used to map the binding area to reside mainly within the hydrophobic pocket of the C-terminal lobe of calmodulin. The solution structure obtained by small-angle X-ray scattering indicates binding of the myelin basic protein peptide into the interlobal groove of calmodulin, while calmodulin remains in an extended conformation.; CONCLUSION: Taken together, our results give a detailed structural insight into the interaction of calmodulin with a C-terminal segment of a major myelin protein, the myelin basic protein. The used 19-mer peptide interacts mainly with the C-terminal lobe of calmodulin, and a conformational change accompanies binding, suggesting a novel mode of calmodulin-target protein interaction. Calmodulin does not collapse and wrap around the peptide tightly; instead, it remains in an extended conformation in the solution structure. The observed affinity can be physiologically relevant, given the high abundance of both binding partners in the nervous system.

登録者

• Maxim Petoukhov (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

モデル

• モデル #63: ; タイプ: atomic / ソフトウェア: Sasref / カイ2乗値: 4.7524; Omokage検索でこの集合体の類似形状データを探す (詳細)

試料

• 試料: 名称: Calmodulin:peptide complex / Sample MW: 18.84 kDa / 試料濃度: 5.30-20.00 / Entity id: 58 / 59
• バッファ: 名称: Tris75 / 濃度: 25.00 mM / pH: 7.5 / 組成: NaCl 200.000 mM

要素 #58

タイプ: protein / 記述: Calmodulin / 分子量: 16.84 / 分子数: 1 / 由来: Homo sapiens / 参照: UniProt: P62158
配列:

MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK

要素 #59

名称: peptide / タイプ: protein / 記述: C-terminal region of human myelin basic protein / 分子量: 2 / 分子数: 1 / 由来: Homo sapiens
配列:

HKGFKGVDAQ GTLSKIFKL

実験情報

• ビーム: 設備名称: DORIS III X33 / 地域: Hamburg / 国: Germany / 線源: X-ray synchrotron
• 検出器: 名称: MAR 345 Image Plate

スキャン

タイトル: CaM:Peptide / 測定日: 2006年11月28日 / 単位: 1/nm /

	Min	Max
Q	0.3198	5.0097

距離分布関数 P(R)

ソフトウェア P(R): GNOM 4.5a / ポイント数: 512 /

	Min	Max
Q	0.3233	4.995
P(R) point	1	512
R	0	7

結果

I0 from Guinier: 107.587 / Rg from Guinier: 2.1 nm / カーブのタイプ: merged /

	実験値	Porod
分子量	20 kDa	-
体積	-	36 nm3

/

	Min	Max
D	-	7
Guinier point	1	85