作者: Emma J Boswell , Nyoman D Kurniawan , A Kristina Downing
DOI: 10.1002/9781119951438.EIBC0513
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摘要: The calcium-binding EGF-like (cbEGF) domain is a common module found in functionally diverse extracellular proteins. Its importance highlighted by number of inherited diseases caused missense mutations within the domain. It characterised six cysteine residues which normally disulphide bond 1–3, 2–4, 5–6 pattern and consensus D/N-x-D/N-E/Q-xm-D/ N*-xn-Y/F (where m n are variables * indicates possible β-hydroxylation). High-resolution structures cbEGF domains have identified fold comprising major minor double- stranded β-hairpins. lacks significant hydrophobic core structure stabilised three bonds calcium binding to amino terminus. Calcium coordinated pentagonal bipyramidal arrangement oxygen atoms, provided intradomain ligands. Each individual contains weak site, affinity may be substantially enhanced N-terminal linkage another Structural analysis linked either homologous or heterologous identifies general role for restricting conformational flexibility interdomain linkages orienting pairs.