Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network

Xianzhong Xu; Surya V.S.R.K. Pulavarti; Alexander Eletsky; Yuanpeng Janet Huang; Thomas B. Acton; Rong Xiao; John K. Everett; Gaetano T. Montelione; Thomas Szyperski

doi:10.1007/s10969-014-9184-z

Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network

Xianzhong Xu
, Surya V.S.R.K. Pulavarti
, Alexander Eletsky
, Yuanpeng Janet Huang
, Thomas B. Acton
, Rong Xiao
, John K. Everett
, Gaetano T. Montelione
, Thomas Szyperski

Chemistry

SUNY Buffalo
Rutgers - The State University of New Jersey, New Brunswick

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

Abstract

High-quality solution NMR structures of three homeodomains from human proteins ALX4, ZHX1 and CASP8AP2 were solved. These domains were chosen as targets of a biomedical theme project pursued by the Northeast Structural Genomics Consortium. This project focuses on increasing the structural coverage of human proteins associated with cancer.

Original language	English
Pages (from-to)	201-207
Number of pages	7
Journal	Journal of Structural and Functional Genomics
Volume	15
Issue number	4
DOIs	https://doi.org/10.1007/s10969-014-9184-z
State	Published - Nov 20 2014

Keywords

Homeodomain
PF00046
Structural genomics
Transcription factor

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10.1007/s10969-014-9184-z

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Xu, X., Pulavarti, S. V. S. R. K., Eletsky, A., Huang, Y. J., Acton, T. B., Xiao, R., Everett, J. K., Montelione, G. T., & Szyperski, T. (2014). Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network. Journal of Structural and Functional Genomics, 15(4), 201-207. https://doi.org/10.1007/s10969-014-9184-z

@article{2b3117200e404a82bad34c6833048df5,

title = "Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network",

abstract = "High-quality solution NMR structures of three homeodomains from human proteins ALX4, ZHX1 and CASP8AP2 were solved. These domains were chosen as targets of a biomedical theme project pursued by the Northeast Structural Genomics Consortium. This project focuses on increasing the structural coverage of human proteins associated with cancer.",

keywords = "Homeodomain, PF00046, Structural genomics, Transcription factor",

author = "Xianzhong Xu and Pulavarti, \{Surya V.S.R.K.\} and Alexander Eletsky and Huang, \{Yuanpeng Janet\} and Acton, \{Thomas B.\} and Rong Xiao and Everett, \{John K.\} and Montelione, \{Gaetano T.\} and Thomas Szyperski",

note = "Publisher Copyright: {\textcopyright} 2014, Springer Science+Business Media Dordrecht.",

year = "2014",

month = nov,

day = "20",

doi = "10.1007/s10969-014-9184-z",

language = "English",

volume = "15",

pages = "201--207",

journal = "Journal of Structural and Functional Genomics",

issn = "1345-711X",

publisher = "Springer Netherlands",

number = "4",

}

Xu, X, Pulavarti, SVSRK, Eletsky, A, Huang, YJ, Acton, TB, Xiao, R, Everett, JK, Montelione, GT & Szyperski, T 2014, 'Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network', Journal of Structural and Functional Genomics, vol. 15, no. 4, pp. 201-207. https://doi.org/10.1007/s10969-014-9184-z

Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network. / Xu, Xianzhong; Pulavarti, Surya V.S.R.K.; Eletsky, Alexander et al.
In: Journal of Structural and Functional Genomics, Vol. 15, No. 4, 20.11.2014, p. 201-207.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network

AU - Xu, Xianzhong

AU - Pulavarti, Surya V.S.R.K.

AU - Eletsky, Alexander

AU - Huang, Yuanpeng Janet

AU - Acton, Thomas B.

AU - Xiao, Rong

AU - Everett, John K.

AU - Montelione, Gaetano T.

AU - Szyperski, Thomas

PY - 2014/11/20

Y1 - 2014/11/20

N2 - High-quality solution NMR structures of three homeodomains from human proteins ALX4, ZHX1 and CASP8AP2 were solved. These domains were chosen as targets of a biomedical theme project pursued by the Northeast Structural Genomics Consortium. This project focuses on increasing the structural coverage of human proteins associated with cancer.

AB - High-quality solution NMR structures of three homeodomains from human proteins ALX4, ZHX1 and CASP8AP2 were solved. These domains were chosen as targets of a biomedical theme project pursued by the Northeast Structural Genomics Consortium. This project focuses on increasing the structural coverage of human proteins associated with cancer.

KW - Homeodomain

KW - PF00046

KW - Structural genomics

KW - Transcription factor

UR - https://www.scopus.com/pages/publications/84911973837

U2 - 10.1007/s10969-014-9184-z

DO - 10.1007/s10969-014-9184-z

M3 - Article

C2 - 24941917

AN - SCOPUS:84911973837

SN - 1345-711X

VL - 15

SP - 201

EP - 207

JO - Journal of Structural and Functional Genomics

JF - Journal of Structural and Functional Genomics

IS - 4

ER -

Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network

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