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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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8 terms
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Biological process
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metabolic process
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24 terms
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Biochemical function
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nucleic acid binding
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14 terms
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DOI no:
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Eur J Biochem
250:712-726
(1997)
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PubMed id:
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Three-dimensional solution structure of human angiogenin determined by 1H,15N-NMR spectroscopy--characterization of histidine protonation states and pKa values.
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O.Lequin,
H.Thüring,
M.Robin,
J.Y.Lallemand.
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ABSTRACT
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Human angiogenin is a member of the pancreatic ribonuclease superfamily that
induces blood vessel formation. Its three-dimensional solution structure has
been determined to high resolution by heteronuclear NMR spectroscopy. 30
structures were calculated, based on a total of 1441 assigned NOE correlations,
64 coupling constants and 50 hydrogen bonds. The backbone atomic rms difference
from the mean coordinates is 0.067 +/- 0.012 nm and 0.13 nm from the previously
determined crystal structure. The side-chain of Gln117 was found to obstruct the
active site as observed in the crystal state. There was no evidence of an
alternative open form of angiogenin, although two sets of chemical shifts were
observed for some residues, mainly around the active site and in the C-terminal
segment. The topology of the ribonucleolytic active site is described with a
particular emphasis on the conformation and protonation of active-site His
residues. The side-chain of His114 adopts two main conformations in solution. In
contrast to pancreatic ribonuclease A, His13 was shown to be more basic than
His114, with pKa values of 6.65 and 6.05 respectively. The His47 residue is
located in an environment very resistant to protonation with a pKa lower than 4.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.La Mendola,
A.Magrì,
L.I.Vagliasindi,
Ã.–.Hansson,
R.P.Bonomo,
and
E.Rizzarelli
(2010).
Copper(II) complex formation with a linear peptide encompassing the putative cell binding site of angiogenin.
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Dalton Trans, 39,
10678-10684.
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V.N.Uversky
(2010).
Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D(2) concept.
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Expert Rev Proteomics, 7,
543-564.
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D.E.Holloway,
G.B.Chavali,
M.C.Hares,
V.Subramanian,
and
K.R.Acharya
(2005).
Structure of murine angiogenin: features of the substrate- and cell-binding regions and prospects for inhibitor-binding studies.
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Acta Crystallogr D Biol Crystallogr, 61,
1568-1578.
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PDB codes:
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Y.R.Pan,
K.P.Wu,
Y.C.Lou,
Y.D.Liao,
and
C.Chen
(2005).
1H, 13C and 15N resonance assignments and secondary structure of murine angiogenin 4.
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J Biomol NMR, 31,
175-176.
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A.Merlino,
L.Vitagliano,
M.A.Ceruso,
and
L.Mazzarella
(2003).
Subtle functional collective motions in pancreatic-like ribonucleases: from ribonuclease A to angiogenin.
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Proteins, 53,
101-110.
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G.B.Chavali,
A.C.Papageorgiou,
K.A.Olson,
J.W.Fett,
G.Hu,
R.Shapiro,
and
K.R.Acharya
(2003).
The crystal structure of human angiogenin in complex with an antitumor neutralizing antibody.
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Structure, 11,
875-885.
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PDB code:
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D.D.Leonidas,
G.B.Chavali,
A.M.Jardine,
S.Li,
R.Shapiro,
and
K.R.Acharya
(2001).
Binding of phosphate and pyrophosphate ions at the active site of human angiogenin as revealed by X-ray crystallography.
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Protein Sci, 10,
1669-1676.
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PDB codes:
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M.S.Madhusudhan,
and
S.Vishveshwara
(2001).
Computer modeling of human angiogenin-dinucleotide substrate interaction.
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Proteins, 42,
125-135.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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