5rhn: Difference between revisions
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[[Image:5rhn.gif|left|200px]] | [[Image:5rhn.gif|left|200px]] | ||
'''HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH 8-BR-AMP''' | {{Structure | ||
|PDB= 5rhn |SIZE=350|CAPTION= <scene name='initialview01'>5rhn</scene>, resolution 2.31Å | |||
|SITE= <scene name='pdbsite=HIT:The+HIS+Triad+Forms+Part+Of+Alpha+Phosphate-Binding+Loop+...'>HIT</scene> | |||
|LIGAND= <scene name='pdbligand=8BR:8-BROMO-ADENOSINE-5'-MONOPHOSPHATE'>8BR</scene> | |||
|ACTIVITY= | |||
|GENE= HINT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus]) | |||
}} | |||
'''HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH 8-BR-AMP''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
5RHN is a [ | 5RHN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5RHN OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9164465 9164465] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nucleotide-binding protein]] | [[Category: nucleotide-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:12:49 2008'' | ||
Revision as of 17:12, 20 March 2008
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| 5rhn, resolution 2.31Å | |||||||||||||
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| Sites: | HIT | ||||||||||||
| Ligands: | 8BR | ||||||||||||
| Gene: | HINT (Oryctolagus cuniculus) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH 8-BR-AMP
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
5RHN is a Single protein structure of sequence from Oryctolagus cuniculus. 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
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