Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1)

FEBS Letters

Kigawa, Takanori²  Yokoyama, Shigeyuki²  Iwahara, Junji²  Koshiba, Seizo²  Kikuchi, Akira¹ 

[1] Department of Biochemistry, Hiroshima University School of Medicine, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8551, Japan;Cellular Signaling Laboratory, The Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan

关键词: POB1;    EH domain;    Calcium-binding protein;    Nuclear magnetic resonance;    Solution structure;    EGF;    epidermal growth factor;    EH;    Eps15 homology;    HSQC;    heteronuclear single quantum coherence;    NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser enhancement;    NOESY;    NOE spectroscopy;    NPF;    Asn-Pro-Phe;    POB1;    partner of RalBP1;    RalBP1;    Ral-binding protein 1;    TOCSY;    total correlated spectroscopy;   

DOI  :  10.1016/S0014-5793(98)01644-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The solution structure of the Eps15 homology (EH) domain of a human POB1 (partner of RalBP1) 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 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.

【 授权许可】

Unknown