1nue

X-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTIONX-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTION

Structural highlights

1nue is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NDKB_HUMAN Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752). Exhibits histidine protein kinase activity.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Iwashita S, Fujii M, Mukai H, Ono Y, Miyamoto M. Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem Biophys Res Commun. 2004 Aug 6;320(4):1063-8. PMID:15249197 doi:http://dx.doi.org/10.1016/j.bbrc.2004.06.067
↑ Wieland T, Hippe HJ, Ludwig K, Zhou XB, Korth M, Klumpp S. Reversible histidine phosphorylation in mammalian cells: a teeter-totter formed by nucleoside diphosphate kinase and protein histidine phosphatase 1. Methods Enzymol. 2010;471:379-402. doi: 10.1016/S0076-6879(10)71020-X. Epub 2010 , Mar 1. PMID:20946858 doi:http://dx.doi.org/10.1016/S0076-6879(10)71020-X

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Iwashita S, Fujii M, Mukai H, Ono Y, Miyamoto M. Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem Biophys Res Commun. 2004 Aug 6;320(4):1063-8. PMID:15249197 doi:http://dx.doi.org/10.1016/j.bbrc.2004.06.067

[2] Wieland T, Hippe HJ, Ludwig K, Zhou XB, Korth M, Klumpp S. Reversible histidine phosphorylation in mammalian cells: a teeter-totter formed by nucleoside diphosphate kinase and protein histidine phosphatase 1. Methods Enzymol. 2010;471:379-402. doi: 10.1016/S0076-6879(10)71020-X. Epub 2010 , Mar 1. PMID:20946858 doi:http://dx.doi.org/10.1016/S0076-6879(10)71020-X

[1]

[2]

1nue

X-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTIONX-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTION

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

1nue

X-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTIONX-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTION

Structural highlights

Function

Evolutionary Conservation

See Also

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Search