This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4rhn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
Histidine triad nucleotide-binding protein (HINT), a dimeric purine, nucleotide-binding protein from rabbit heart, is a member of the HIT, (histidine triad) superfamily which includes HINT homologues and FHIT (HIT, protein encoded at the chromosome 3 fragile site) homologues. Crystal, structures of HINT-nucleotide complexes demonstrate that the most, conserved residues in the superfamily mediate nucleotide binding and that, the HIT motif forms part of the phosphate binding loop., Galactose-1-phosphate uridylyltransferase, whose deficiency causes, galactosemia, contains tandem HINT domains with the same fold and mode of, nucleotide binding as HINT despite having no overall sequence similarity., Features of FHIT, a diadenosine polyphosphate hydrolase and candidate, tumour suppressor, are predicted from HINT-nucleotide structures.
+
Histidine triad nucleotide-binding protein (HINT), a dimeric purine nucleotide-binding protein from rabbit heart, is a member of the HIT (histidine triad) superfamily which includes HINT homologues and FHIT (HIT protein encoded at the chromosome 3 fragile site) homologues. Crystal structures of HINT-nucleotide complexes demonstrate that the most conserved residues in the superfamily mediate nucleotide binding and that the HIT motif forms part of the phosphate binding loop. Galactose-1-phosphate uridylyltransferase, whose deficiency causes galactosemia, contains tandem HINT domains with the same fold and mode of nucleotide binding as HINT despite having no overall sequence similarity. Features of FHIT, a diadenosine polyphosphate hydrolase and candidate tumour suppressor, are predicted from HINT-nucleotide structures.
==About this Structure==
==About this Structure==
Line 16: Line 16:
[[Category: Garrison, P.]]
[[Category: Garrison, P.]]
[[Category: Gilmour, J.]]
[[Category: Gilmour, J.]]
-
[[Category: Lowenstein, J.M.]]
+
[[Category: Lowenstein, J M.]]
[[Category: Peisach, D.]]
[[Category: Peisach, D.]]
-
[[Category: Petsko, G.A.]]
+
[[Category: Petsko, G A.]]
[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
[[Category: RIB]]
[[Category: RIB]]
[[Category: nucleotide-binding protein]]
[[Category: nucleotide-binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:53:08 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:14:10 2008''

Revision as of 17:14, 21 February 2008


4rhn, resolution 1.90Å

Drag the structure with the mouse to rotate

HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH ADENOSINE

Overview

Histidine triad nucleotide-binding protein (HINT), a dimeric purine nucleotide-binding protein from rabbit heart, is a member of the HIT (histidine triad) superfamily which includes HINT homologues and FHIT (HIT protein encoded at the chromosome 3 fragile site) homologues. Crystal structures of HINT-nucleotide complexes demonstrate that the most conserved residues in the superfamily mediate nucleotide binding and that the HIT motif forms part of the phosphate binding loop. Galactose-1-phosphate uridylyltransferase, whose deficiency causes galactosemia, contains tandem HINT domains with the same fold and mode of nucleotide binding as HINT despite having no overall sequence similarity. Features of FHIT, a diadenosine polyphosphate hydrolase and candidate tumour suppressor, are predicted from HINT-nucleotide structures.

About this Structure

4RHN is a Single protein structure of sequence from Oryctolagus cuniculus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins., Brenner C, Garrison P, Gilmour J, Peisach D, Ringe D, Petsko GA, Lowenstein JM, Nat Struct Biol. 1997 Mar;4(3):231-8. PMID:9164465

Page seeded by OCA on Thu Feb 21 19:14:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools