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

J Struct Funct Genomics. 2014 Dec;15(4):201-7. doi: 10.1007/s10969-014-9184-z. Epub 2014 Jun 19.

Authors

Xianzhong Xu¹, Surya V S R K Pulavarti, Alexander Eletsky, Yuanpeng Janet Huang, Thomas B Acton, Rong Xiao, John K Everett, Gaetano T Montelione, Thomas Szyperski

Affiliation

¹ Department of Chemistry, The State University of New York at Buffalo and Northeast Structural Genomics Consortium, Buffalo, NY, 14260, USA.

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.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

Apoptosis Regulatory Proteins / chemistry*
Calcium-Binding Proteins / chemistry*
DNA-Binding Proteins / chemistry*
Homeodomain Proteins / chemistry*
Humans
Neoplasm Proteins / chemistry*
Neoplasms / chemistry*
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Tertiary
Transcription Factors / chemistry*

Substances

ALX4 protein, human
Apoptosis Regulatory Proteins
CASP8AP2 protein, human
Calcium-Binding Proteins
DNA-Binding Proteins
Homeodomain Proteins
Neoplasm Proteins
Transcription Factors
ZHX1 protein, human

Grants and funding

U54 GM094597/GM/NIGMS NIH HHS/United States