We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1nue

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nue.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1nue.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nue| PDB=1nue | SCENE= }}
{{STRUCTURE_1nue| PDB=1nue | SCENE= }}
-
'''X-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTION'''
+
===X-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
BACKGROUND: Nucleoside diphosphate (NDP) kinases provide precursors for DNA and RNA synthesis. In mammals, these enzymes are also involved in cell regulations. Human NDP kinase B, product of the human nm23-H2 gene, is both an enzyme and a transcription factor. It activates transcription of the c-myc oncogene independently of its catalytic function, by binding to its promoter DNA. How do the two functions coexist? RESULTS: Recombinant human NDP kinase B was co-crystallized with GDP. The X-ray structure was solved at 2.0 A resolution by molecular replacement from the homologous Drosophila Awd protein. Both enzymes are homo-hexamers with a characteristic beta alpha beta beta alpha beta fold. GDP binds near the active site His118. The guanine base is in a surface cleft and interacts with the C terminus of another subunit. CONCLUSIONS: The beta alpha beta beta alpha beta fold, also present in the 'palm' domain of Escherichia coli DNA polymerase I and HIV reverse transcriptase, is both a mononucleotide- and a polynucleotide-binding fold. If NDP kinase B binds DNA in the same way as the polymerases, the enzyme must undergo a conformation change in order to carry out gene activation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8747457}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8747457 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8747457}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Nucleoside diphosphate]]
[[Category: Nucleoside diphosphate]]
[[Category: Nucleoside triphosphate]]
[[Category: Nucleoside triphosphate]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:59:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:08:18 2008''

Revision as of 07:08, 28 July 2008

Image:1nue.png

Template:STRUCTURE 1nue

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

Template:ABSTRACT PUBMED 8747457

About this Structure

1NUE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution., Morera S, Lacombe ML, Xu Y, LeBras G, Janin J, Structure. 1995 Dec 15;3(12):1307-14. PMID:8747457

Page seeded by OCA on Mon Jul 28 10:08:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nue"
Personal tools