The average conformation at micromolar [Ca2+] of Ca2+-atpase with bound nucleotide differs from that adopted with the transition state analog ADP.AlFx or with AMPPCP under crystallization conditions at millimolar [Ca2+].
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SERCA mutant E309Q binds two Ca2+ions but adopts a catalytically incompetent conformationDetermination of the dissociation constants for Ca2+ and calmodulin from the plasma membrane Ca2+ pump by a lipid probe that senses membrane domain changes.Concerted but noncooperative activation of nucleotide and actuator domains of the Ca-ATPase upon calcium binding.Concerted conformational effects of Ca2+ and ATP are required for activation of sequential reactions in the Ca2+ ATPase (SERCA) catalytic cycle.Crystal structure of D351A and P312A mutant forms of the mammalian sarcoplasmic reticulum Ca(2+) -ATPase reveals key events in phosphorylation and Ca(2+) release.Changes in electrostatic surface potential of Na+/K+-ATPase cytoplasmic headpiece induced by cytoplasmic ligand(s) binding.Formation of the stable structural analog of ADP-sensitive phosphoenzyme of Ca2+-ATPase with occluded Ca2+ by beryllium fluoride: structural changes during phosphorylation and isomerization.Effects of inhibitors on luminal opening of Ca2+ binding sites in an E2P-like complex of sarcoplasmic reticulum Ca22+-ATPase with Be22+-fluoride.Critical role of Val-304 in conformational transitions that allow Ca2+ occlusion and phosphoenzyme turnover in the Ca2+ transport ATPase.Comprehensive analysis of expression and function of 51 sarco(endo)plasmic reticulum Ca2+-ATPase mutants associated with Darier disease.Structural and Biochemical Studies on the Reaction Mechanism of Uridine-Cytidine Kinase.
P2860
Q27680675-0642A6BD-F61A-40EA-929C-4AEC84869C43Q33581158-52A1645D-599B-4C4F-B2AD-99F552D8EC9FQ35609827-537B88A4-D8BC-4D7F-8430-35D57B55F9C9Q36851517-1325D8FB-69C4-4967-BE5E-D5B5D4495F2CQ40000056-6BACE0FA-0CFA-4FC9-B3DC-4B02A91F5142Q42551781-30A4D291-3FD8-48E5-8B77-7EFB01332CD2Q42575051-21CC00E8-F1C0-4A42-BC47-C5873ACC6856Q46839427-0073E1CA-AA29-443F-B321-B5235A644298Q46868199-5FF01169-EF4B-4EED-B044-8D4F3B6B6313Q52571382-6FAD6E31-3133-45E6-8934-4839FA0FE802Q53462281-56D170AD-1CAE-49CC-8AA8-D47FEC06E036
P2860
The average conformation at micromolar [Ca2+] of Ca2+-atpase with bound nucleotide differs from that adopted with the transition state analog ADP.AlFx or with AMPPCP under crystallization conditions at millimolar [Ca2+].
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
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name
The average conformation at mi ...... nditions at millimolar [Ca2+].
@en
The average conformation at mi ...... nditions at millimolar [Ca2+].
@nl
type
label
The average conformation at mi ...... nditions at millimolar [Ca2+].
@en
The average conformation at mi ...... nditions at millimolar [Ca2+].
@nl
prefLabel
The average conformation at mi ...... nditions at millimolar [Ca2+].
@en
The average conformation at mi ...... nditions at millimolar [Ca2+].
@nl
P2860
P356
P1476
The average conformation at mi ...... nditions at millimolar [Ca2+].
@en
P2093
Chikashi Toyoshima
Philippe Champeil
P2860
P304
18745-18754
P356
10.1074/JBC.M501596200
P407
P577
2005-03-09T00:00:00Z