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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Abstract	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.
AbstractList	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. 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. 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.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.
Author	Swindells, Mark B. Yap, Kyoko L. Ikura, Mitsuhiko Ames, James B.
Author_xml	– sequence: 1 givenname: Kyoko L. surname: Yap fullname: Yap, Kyoko L. organization: Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, Canada – sequence: 2 givenname: James B. surname: Ames fullname: Ames, James B. organization: Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland – sequence: 3 givenname: Mark B. surname: Swindells fullname: Swindells, Mark B. organization: Inpharmatica, London,United Kingdom – sequence: 4 givenname: Mitsuhiko surname: Ikura fullname: Ikura, Mitsuhiko email: mikura@oci.utoronto.ca organization: Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, Canada
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/10591109$$D View this record in MEDLINE/PubMed
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Snippet	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+... 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+...
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SubjectTerms	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
Title	Diversity of conformational states and changes within the EF-hand protein superfamily
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