Premium
Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1)
Author(s) -
Koshiba Seizo,
Kigawa Takanori,
Iwahara Junji,
Kikuchi Akira,
Yokoyama Shigeyuki
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01644-5
Subject(s) - heteronuclear molecule , calmodulin , homology (biology) , calcium , troponin c , crystallography , chemistry , calcium binding protein , nuclear magnetic resonance spectroscopy , stereochemistry , biochemistry , troponin , amino acid , psychology , organic chemistry , psychiatry , myocardial infarction
The solution structure of the Eps15 homology (EH) domain of a human POB1 (partner of RalBP1) has been determined by uniform 13 C/ 15 N 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 α‐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.