efhand_Ca_insenCa2+ insensitive EF hand |
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| SMART accession number: | SM01184
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| Description: |
EF hands are helix-loop-helix binding motifs involved in the regulation of many cellular processes. EF hands usually bind to Ca2+ ions which causes a major conformational change that allows the protein to interact with its designated targets. This domain corresponds to an EF hand which has partially or entirely lost its calcium-binding properties. The calcium insensitive EF hand is still able to mediate protein-protein recognition (PUBMED:11573089). |
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There are 315
efhand_Ca_insen domains in 315 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Cellular role (predicted cellular role)
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Cellular role: signalling
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Atkinson RA et al.
- Ca2+-independent binding of an EF-hand domain to a novel motif in thealpha-actinin-titin complex.
- Nat Struct Biol. 2001; 8: 853-7
- Display abstract
The interaction between alpha-actinin and titin, two modular muscle proteins, is essential for sarcomere assembly. We have solved the solution structure of acomplex between the calcium-insensitive C-terminal EF-hand domain ofalpha-actinin-2 and the seventh Z-repeat of titin. The structure of the complexis in a semi-open conformation and closely resembles that of myosin light chains in their complexes with heavy chain IQ motifs. However, no IQ motif is present inthe Z-repeat, suggesting that the semi-open conformation is a general structural solution for calcium-independent recognition of EF-hand domains.
- Structure (3D structures containing this domain)
3D Structures of efhand_Ca_insen domains in PDB
| PDB code | Main view | Title | | 1h8b |  | Ef-hands 3,4 from alpha-actinin / z-repeat 7 from titin |
| 1sjj |  | Cryo-em structure of chicken gizzard smooth muscle alpha- actinin |
- Links (links to other resources describing this domain)
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