Diversity of conformational states and changes within the EF-hand protein superfamily

The EF‐hand motif, which assumes a helix‐loop‐helix structure normally responsible for Ca2+ binding, is found in a large number of functionally diverse Ca2+ binding proteins collectively known as the EF‐hand protein superfamily. In many superfamily members, Ca2+ binding induces a conformational chan...

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Veröffentlicht in:Proteins, structure, function, and bioinformatics Jg. 37; H. 3; S. 499 - 507
Hauptverfasser: Yap, Kyoko L., Ames, James B., Swindells, Mark B., Ikura, Mitsuhiko
Format: Journal Article
Sprache:Englisch
Veröffentlicht: New York John Wiley & Sons, Inc 15.11.1999
Schlagworte:
Amino Acid Motifs
Calcium Signaling
Calcium-Binding Proteins - chemistry
Calmodulin - chemistry
conformational change
EF-hand protein
Helix-Loop-Helix Motifs
Molecular Conformation
Protein Conformation
Troponin C - chemistry
ISSN:0887-3585, 1097-0134
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Zusammenfassung:The EF‐hand motif, which assumes a helix‐loop‐helix structure normally responsible for Ca2+ binding, is found in a large number of functionally diverse Ca2+ binding proteins collectively known as the EF‐hand protein superfamily. In many superfamily members, Ca2+ binding induces a conformational change in the EF‐hand motif, leading to the activation or inactivation of target proteins. In calmodulin and troponin C, this is described as a change from the closed conformational state in the absence of Ca2+ to the open conformational state in its presence. It is now clear from structures of other EF‐hand proteins that this “closed‐to‐open” conformational transition is not the sole model for EF‐hand protein structural response to Ca2+. More complex modes of conformational change are observed in EF‐hand proteins that interact with a covalently attached acyl group (e.g., recoverin) and in those that dimerize (e.g., S100B, calpain). In fact, EF‐hand proteins display a multitude of unique conformational states, together constituting a conformational continuum. Using a quantitative 3D approach termed vector geometry mapping (VGM), we discuss this tertiary structural diversity of EF‐hand proteins and its correlation with target recognition. Proteins 1999;37:499–507. ©1999 Wiley‐Liss, Inc.
Bibliographie:Medical Research Council of Canada
ark:/67375/WNG-X8ZNJ759-Q
National Institutes of Health - No. EY-12347
ArticleID:PROT17
istex:253A2461603372618DF05504B86F97692018D3A9
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
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ISSN:0887-3585
1097-0134
DOI:10.1002/(SICI)1097-0134(19991115)37:3<499::AID-PROT17>3.0.CO;2-Y