Structural Changes of the Sarcoplasmic Reticulum Ca(II)-ATPase Nucleotide Binding Domain by pH and La(III)

1997 ◽  
Vol 348 (1) ◽  
pp. 152-156 ◽  
Author(s):  
Jaime M. Merino ◽  
Fernando Henao ◽  
Carlos Gutiérrez-Merino
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Structural Changes ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain

scholarly journals Definition of surface-exposed epitopes on the (Ca2+-Mg2+)-ATPase of sarcoplasmic reticulum

1991 ◽  
Vol 279 (1) ◽  
pp. 203-212 ◽  
Author(s):  
R E A Tunwell ◽  
J W Conlan ◽  
I Matthews ◽  
J M East ◽  
A G Lee
Keyword(s):  
Monoclonal Antibodies ◽  
Sarcoplasmic Reticulum ◽  
Polyclonal Antibodies ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Stalk Domain ◽  
Definition Of ◽  
Peptide Antibodies

Epitopes for monoclonal antibodies binding to the native (Ca(2+)-Mg2+)-ATPase have been defined by studying binding to sets of hexameric peptides synthesized on plastic pegs. Epitopes have been confirmed by demonstrating the binding of anti-peptide antibodies to the ATPase. A method is presented for definition of surface-exposed epitopes using polyclonal antibodies. Three surface-exposed epitopes have been defined in the nucleotide-binding domain of the ATPase, suggesting considerable surface exposure of this region. Other surface-exposed epitopes have been located in the region of the fourth stalk domain.

scholarly journals Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides

2010 ◽  
Vol 66 (9) ◽  
pp. 979-987 ◽  
Author(s):  
Matthias Haffke ◽  
Anja Menzel ◽  
Yvonne Carius ◽  
Dieter Jahn ◽  
Dirk W. Heinz
Keyword(s):  
Abc Transporters ◽  
Structural Changes ◽  
Catalytic Mechanism ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Full Length ◽  
Nucleotide Binding Domain ◽  
Structural Comparison ◽  
Insight Into

The human ATP-binding cassette (ABC) transporter ABCB6 is involved in haem-precursor transport across the mitochondrial membrane. The crystal structure of its nucleotide-binding domain (NBD) has been determined in the apo form and in complexes with ADP, with ADP and Mg2+ and with ATP at high resolution. The overall structure is L-shaped and consists of two lobes, consistent with other reported NBD structures. Nucleotide binding is mediated by the highly conserved Tyr599 and the Walker A motif, and induces notable structural changes. Structural comparison with other structurally characterized NBDs and full-length ABC transporters gives the first insight into the possible catalytic mechanism of ABCB6 and the role of the N-terminal helix α1 in full-length ABCB6.

scholarly journals A possible nucleotide-binding domain in the tertiary fold of phosphoribosyltransferases.

1983 ◽  
Vol 258 (10) ◽  
pp. 6450-6457 ◽  
Author(s):  
P Argos ◽  
M Hanei ◽  
J M Wilson ◽  
W N Kelley
Keyword(s):  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain
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