UMLS. CSP-HL7-ICD9CM-NCI-NDFRT-RXNORM
%
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
E E0 E6 E7 EA EB EC ED EE EF EG EH EI EJ EK EL EM EN EO EP EQ ER ES ET EU EV EW EX EY
EFA EFF EFH EFL EFO EFP EFT EFU

EF hand

[Forming a single Ca2+-binding site in many calcium-binding proteins, the basic EF-Hand Domain consists of a conserved 12-residue loop region between two perpendicular 10-12 residue alpha helices (helix-loop-helix). Ca2+ interacts with loop residues in a pentagonal bipyramidal configuration; each loop residue is important for Ca2+ coordination. Loop residues 1, 3, 5, 7, 9, and 12 (invariant Glu or Asp) are directly necessary for Ca2+ binding. Amino-acid variations at positions 1, 3, 5, 7, and 9 alter ion affinity. Single or multiple domains cause structural/functional variations. EF-hand Proteins are grouped into either regulatory/signaling or structural/buffering/transport categories. Ca2+ binding to regulatory proteins induces conformational/functional change; Ca2+ binding to structural proteins seems to provide a Ca2+ buffer. (NCI) ( NCI )]
UMLS (CSP) C0752218
EF-Hand Calcium-Binding Motif
EF-Hand Domain
EF-Hand Motif
 
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