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

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

doi:10.1016/S0014-5793(98)01644-5

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 journal › Article › peer-review

24 Scopus citations

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 language	English (US)
Pages (from-to)	138-142
Number of pages	5
Journal	FEBS Letters
Volume	442
Issue number	2-3
DOIs	https://doi.org/10.1016/S0014-5793(98)01644-5
State	Published - Jan 15 1999
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(98)01644-5

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title = "Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1)",

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.",

keywords = "Calcium-binding protein, EH domain, Nuclear magnetic resonance, POB1, Solution structure",

author = "Seizo Koshiba and Takanori Kigawa and Junji Iwahara and Akira Kikuchi and Shigeyuki Yokoyama",

note = "Funding Information: We thank Drs. K. Takio and N. Domae for performing the mass spectrometry. We also thank Dr. M. Shirouzu for many helpful discussions. This work was supported by Grants-in-Aid from the Ministry of Education, Science, Sports and Culture, Japan.",

year = "1999",

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doi = "10.1016/S0014-5793(98)01644-5",

language = "English (US)",

volume = "442",

pages = "138--142",

journal = "FEBS Letters",

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T1 - Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1)

AU - Koshiba, Seizo

AU - Kigawa, Takanori

AU - Iwahara, Junji

AU - Kikuchi, Akira

AU - Yokoyama, Shigeyuki

N1 - Funding Information: We thank Drs. K. Takio and N. Domae for performing the mass spectrometry. We also thank Dr. M. Shirouzu for many helpful discussions. This work was supported by Grants-in-Aid from the Ministry of Education, Science, Sports and Culture, Japan.

PY - 1999/1/15

Y1 - 1999/1/15

N2 - 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.

AB - 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.

KW - Calcium-binding protein

KW - EH domain

KW - Nuclear magnetic resonance

KW - POB1

KW - Solution structure

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U2 - 10.1016/S0014-5793(98)01644-5

DO - 10.1016/S0014-5793(98)01644-5

M3 - Article

C2 - 9928989

AN - SCOPUS:0032908611

SN - 0014-5793

VL - 442

SP - 138

EP - 142

JO - FEBS Letters

JF - FEBS Letters

IS - 2-3

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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