1988
DOI: 10.1016/0022-2836(88)90608-0
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Structure of calmodulin refined at 2.2 Å resolution

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Cited by 1,086 publications
(1,113 citation statements)
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References 37 publications
(9 reference statements)
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“…The Ile-27 residue is one that participates in the hydrophobic cleft that is exposed upon Ca2+ binding (Babu et al, 1985(Babu et al, , 1988. If chemical shift changes of Ile-27 CyH, are indicative of formation of the hydrophobic cleft, then the results shown here suggest that the binding of a single calcium ion in either site in the N-terminal domain can activate the conformational "switch" that organizes the residues involved in forming the hydrophobic cleft.…”
Section: Conformational Effectsmentioning
confidence: 82%
See 1 more Smart Citation
“…The Ile-27 residue is one that participates in the hydrophobic cleft that is exposed upon Ca2+ binding (Babu et al, 1985(Babu et al, , 1988. If chemical shift changes of Ile-27 CyH, are indicative of formation of the hydrophobic cleft, then the results shown here suggest that the binding of a single calcium ion in either site in the N-terminal domain can activate the conformational "switch" that organizes the residues involved in forming the hydrophobic cleft.…”
Section: Conformational Effectsmentioning
confidence: 82%
“…The CaHs from Thr-26 and Asp-64 are positioned directly across from each other in a region of 0-sheet that lies between sites I and I1 (Kinemage 4; Babu et al, 1985Babu et al, , 1988Seeholzer & Wand, 1989). In wild-type CaM, these peaks titrate upfield almost simultaneously in fast exchange with midpoints of the change in chemical shift observed at 3.1 (Thr-26) and 3.0 (Asp-64) equivalents of Ca2+ (Fig.…”
Section: Site I and Ii Mutantsmentioning
confidence: 96%
“…Succinimide formation at Asp and Asn is thus highly regulated by three-dimensional structure, due to the requirement that the peptide nitrogen atom be in a position to attack the side-chain carbonyl of the Asx residue [72]. The Ca# + -calmodulin crystal structure indicates that the peptide-bond nitrogen of Thr-79 is not in a position to attack the side-chain carbonyl carbon of Asp-78 and form a succinimide [90] ; however, for calmodulin, the crystal structure [90] and solution studies [91] indicate that Asp-78 and Thr-79 are in flexible regions, allowing succinimide formation. The location of the labile Asp-2 is the flexible N-terminal region of calmodulin [89].…”
Section: Aspartate Residuesmentioning
confidence: 99%
“…This is in sharp contrast to other calcium binding proteins such as calmodulin (25,26), troponin C (27,28), and calbindin (29) or other Gla-containing proteins (1)(2)(3). A high-resolution structure of Ca 2+ -osteocalcin will provide information on a new class of proteins.…”
mentioning
confidence: 96%