The Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner.
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The distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104FCOMMD1 forms oligomeric complexes targeted to the endocytic membranes via specific interactions with phosphatidylinositol 4,5-bisphosphateBiochemical basis of regulation of human copper-transporting ATPasesMolecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypesSingle-molecule dynamics and mechanisms of metalloregulators and metallochaperonesStructural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilisStructure of a Copper Pump Suggests a Regulatory Role for Its Metal-Binding DomainNucleotide recognition by CopA, a Cu+-transporting P-type ATPaseMechanistic insights into Cu(I) cluster transfer between the chaperone CopZ and its cognate Cu(I)-transporting P-type ATPase, CopAStructure and interactions of the C-terminal metal binding domain of Archaeoglobus fulgidus CopAThe Architecture of CopA from Archeaoglobus fulgidus Studied by Cryo-Electron Microscopy and Computational DockingCyanobacterial metallochaperone inhibits deleterious side reactions of copperConformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycleStructural biology of copper traffickingCopper metallochaperonesElucidation of the ATP7B N-domain Mg2+-ATP coordination site and its allosteric regulationIn silico investigation of the ATP7B gene: insights from functional prediction of non-synonymous substitution to protein structure.Metal binding to the N-terminal cytoplasmic domain of the PIB ATPase HMA4 is required for metal transport in Arabidopsis.Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B.The loop connecting metal-binding domains 3 and 4 of ATP7B is a target of a kinase-mediated phosphorylationDiversity of the metal-transporting P1B-type ATPasesDiverse functional properties of Wilson disease ATP7B variants.A conditional mutation affecting localization of the Menkes disease copper ATPase. Suppression by copper supplementation.The transport mechanism of bacterial Cu+-ATPases: distinct efflux rates adapted to different function.Critical roles for the COOH terminus of the Cu-ATPase ATP7B in protein stability, trans-Golgi network retention, copper sensing, and retrograde trafficking.Zn, Cu and Co in cyanobacteria: selective control of metal availability.Wilson's disease: a comprehensive review of the molecular mechanisms.Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.Communication between the N and C termini is required for copper-stimulated Ser/Thr phosphorylation of Cu(I)-ATPase (ATP7B).Evolution of copper transporting ATPases in eukaryotic organisms.Functional and Biochemical Characterization of Cucumber Genes Encoding Two Copper ATPases CsHMA5.1 and CsHMA5.2.Molecular events initiating exit of a copper-transporting ATPase ATP7B from the trans-Golgi networkCopper transportion of WD protein in hepatocytes from Wilson disease patients in vitroToward a molecular understanding of metal transport by P(1B)-type ATPases.The mechanism of Cu+ transport ATPases: interaction with CU+ chaperones and the role of transient metal-binding sites.Structural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA.Common patterns and unique features of P-type ATPases: a comparative view on the KdpFABC complex from Escherichia coli (Review).Apical targeting and Golgi retention signals reside within a 9-amino acid sequence in the copper-ATPase, ATP7B.Sinorhizobium meliloti Nia is a P(1B-5)-ATPase expressed in the nodule during plant symbiosis and is involved in Ni and Fe transport.Chaperone-mediated Cu+ delivery to Cu+ transport ATPases: requirement of nucleotide binding.
P2860
Q24297174-BDC9B47E-DEAA-4F92-ACCF-58E79BA937FDQ24336648-5CEBB87C-C5AA-4578-B944-12F3A816195DQ24569563-84134564-F57F-4C6B-B0F1-18CCB36F6B09Q24647056-F0354D25-8A92-453F-93F8-99D688422189Q27001348-C075B13A-11F7-4781-A17B-AABB87CD9023Q27642229-DBED6ADA-8057-4995-86F9-FFCFAD8EB2A0Q27650803-A50111CD-7DA8-4110-9271-466178A76D42Q27655678-5A21A9FF-47D8-4E99-938E-9544569F9938Q27657429-DE6B62C3-DAC1-45B6-8EF4-02C45B6D742EQ27663110-03252FD4-A0B3-4BF0-AB38-58702314F95DQ27671559-60A29318-C3ED-48CF-B8A1-F327D50160E0Q27676458-DEC8FEF4-B3DE-477D-9A55-EFDDED06285EQ27679487-9E5EAE98-6F83-4C4A-A0B2-7B7C3368182FQ28261249-5071508C-1B9F-4844-A023-49947BB46A48Q28275083-D25B2D27-0939-423B-9E1B-B5919050D08DQ28743427-D608C0B4-7C80-4F05-B510-C43C176E7865Q30355775-ADDFCEEF-AF49-49D4-96AC-EACA06CCFAE0Q30383754-F7D9FF0B-8C03-44E8-8F58-7C7B30993824Q33673628-B328EDE1-81BD-42AD-AE5A-8D35566AE998Q33706048-74C8C7CD-C32F-4754-AF65-EE567E68D207Q33992452-F245E846-85CF-4E40-A222-5880396043D0Q34125926-484D6D73-2955-4AE0-B2C3-D1F79B4D123CQ34148762-0B96FECB-189F-41BC-BA76-0557C69C352CQ34970478-B8CD39B7-4BC0-42A4-BA24-4134EA2FB785Q35087086-07E230B2-FCE3-4F5F-907C-4D245A2535A9Q35164010-A3B872B3-147C-4E93-AF90-33D7AB9AB97DQ35381754-185A0568-13B5-4CD7-ABBE-6E4651A20615Q35574986-ED632418-E998-4EE7-A4CB-ACBAF5A2197DQ35580770-2A937DBF-1602-4029-8C66-26D1E99D08B3Q35841316-660816D0-99E7-48DE-9E06-7DBD5D8120D2Q35860696-9E9D1777-F271-46C7-BCD2-9018CE375101Q36332811-4FFB3401-3014-4245-9652-A5E553D6A25DQ36415720-654D7436-22A0-428D-BBC9-FE732CC68D38Q36432934-11C7F61A-12EF-4C99-AAB0-34E72FC6032AQ36508768-908DB8C0-09E3-4EAB-BC60-DEF77BD39814Q36583819-791612C3-9304-42C9-8D26-319612E7F11AQ36915232-876E594C-BCC6-4AD8-95F5-F21BF5EA0BCEQ37100260-0172C59C-F2F2-4389-9653-224E7212C8FBQ37337203-F2CACFF2-B53B-4600-A504-F3E5C4C12E0BQ37344036-FCBA65D9-2D8A-4684-8CBA-29C4FFB34D80
P2860
The Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner.
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The Lys1010-Lys1325 fragment o ...... in a copper-dependent manner.
@ast
The Lys1010-Lys1325 fragment o ...... in a copper-dependent manner.
@en
type
label
The Lys1010-Lys1325 fragment o ...... in a copper-dependent manner.
@ast
The Lys1010-Lys1325 fragment o ...... in a copper-dependent manner.
@en
prefLabel
The Lys1010-Lys1325 fragment o ...... in a copper-dependent manner.
@ast
The Lys1010-Lys1325 fragment o ...... in a copper-dependent manner.
@en
P2093
P2860
P356
P1476
The Lys1010-Lys1325 fragment o ...... in a copper-dependent manner.
@en
P2093
Lutsenko S
MacArthur BC
Tsivkovskii R
P2860
P304
P356
10.1074/JBC.M003238200
P407
P577
2000-10-25T00:00:00Z