Abstract
The solution structure of the Eps15 homology (EH) domain of a human POB1 (partner of RaIBP1) has been determined by uniform 13C/15N labeling and heteronuclear multidimensional nuclear magnetic resonance spectroscopy. The POB1 EH domain consists of two EF-hand structures, and the second one binds a calcium ion. In the calcium-bound state, the orientation of the fourth alpha-helix relative to the other helices of the POB1 EH domain is slightly different from that of calbindin, and much more different from those of calmodulin and troponin C, on the basis of their atomic coordinates.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing
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Amino Acid Sequence
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Calcium / metabolism
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Calcium / pharmacology
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Calcium-Binding Proteins / chemistry*
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / metabolism
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Edetic Acid / pharmacology
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Helix-Loop-Helix Motifs
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Humans
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Intracellular Signaling Peptides and Proteins*
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Phosphoproteins / chemistry*
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Proline / metabolism
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Protein Denaturation / drug effects
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Sequence Homology, Amino Acid*
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Thermodynamics
Substances
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Adaptor Proteins, Signal Transducing
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Calcium-Binding Proteins
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DNA-Binding Proteins
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EPS15 protein, human
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Intracellular Signaling Peptides and Proteins
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Phosphoproteins
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REPS2 protein, human
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Proline
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Edetic Acid
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Calcium