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

Seizo Koshiba, Takanori Kigawa, Junji Iwahara, Akira Kikuchi, Shigeyuki Yokoyama

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

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. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)138-142
Number of pages5
JournalFEBS Letters
Volume442
Issue number2-3
DOIs
StatePublished - Jan 15 1999
Externally publishedYes

Fingerprint

Troponin C
Biomolecular Nuclear Magnetic Resonance
Calcium
EF Hand Motifs
Calbindins
Calmodulin
Labeling
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
Ions

Keywords

  • Calcium-binding protein
  • EH domain
  • Nuclear magnetic resonance
  • POB1
  • Solution structure

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1). / Koshiba, Seizo; Kigawa, Takanori; Iwahara, Junji; Kikuchi, Akira; Yokoyama, Shigeyuki.

In: FEBS Letters, Vol. 442, No. 2-3, 15.01.1999, p. 138-142.

Research output: Contribution to journalArticle

Koshiba, Seizo ; Kigawa, Takanori ; Iwahara, Junji ; Kikuchi, Akira ; Yokoyama, Shigeyuki. / Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1). In: FEBS Letters. 1999 ; Vol. 442, No. 2-3. pp. 138-142.
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