2012
DOI: 10.1016/j.jmb.2011.10.037
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Decoding the Molecular Design Principles Underlying Ca2+ Binding to βγ-Crystallin Motifs

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Cited by 21 publications
(46 citation statements)
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“…WmKT, SKLP, and SMPI) were identified based on structural similarity (34 -36); these did not belong to the ␤␥-crystallins lineage and may have arisen from convergent evolution (37). With the advent of genomic sequence information, many members from diverse species (bacteria, archaea, and urochordate) were added to the superfamily and also confirmed to be Ca 2ϩ -binding proteins (22, 23, 38 -43), leading to the recognition of a common motif for ion binding, and thus prompting the organization of these proteins as a separate set of Ca 2ϩ -binding proteins (23,44).…”
Section: ␤␥-Crystallins and Ca 2؉ Binding: A Chronologymentioning
confidence: 99%
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“…WmKT, SKLP, and SMPI) were identified based on structural similarity (34 -36); these did not belong to the ␤␥-crystallins lineage and may have arisen from convergent evolution (37). With the advent of genomic sequence information, many members from diverse species (bacteria, archaea, and urochordate) were added to the superfamily and also confirmed to be Ca 2ϩ -binding proteins (22, 23, 38 -43), leading to the recognition of a common motif for ion binding, and thus prompting the organization of these proteins as a separate set of Ca 2ϩ -binding proteins (23,44).…”
Section: ␤␥-Crystallins and Ca 2؉ Binding: A Chronologymentioning
confidence: 99%
“…An analysis of Ͼ100 sequences of canonical motifs available demonstrated that the amino acid residues forming the (N/D)(N/D)XX(S/T)S fingerprint vary in various proteins of the superfamily (44). The first residue of the fingerprint is involved in stabilizing the pocket through hydrogen bonding with the hydroxyl side chain of Ca 2ϩ coordinating Ser/Thr and in some cases supports a water molecule present at the Ϫy position.…”
Section: Preferred Residues In the Binding Motif And Their Significancementioning
confidence: 99%
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