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* Residue conservation analysis
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Enzyme class:
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Chains A, B, C, D:
E.C.?
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J Mol Biol
233:270-274
(1993)
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PubMed id:
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Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure at 2.5 A resolution.
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V.Richard,
G.G.Dodson,
Y.Mauguen.
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ABSTRACT
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The haemoglobin-2,3-diphosphoglycerate complex structure has been solved at 2.5
A resolution using crystals grown from low-salt solutions. The results show some
important differences with the precedent haemoglobin-2,3-diphosphoglycerate
high-salt structure solved by Arnone. First, we observe a loss of symmetry in
the binding site, secondly both of the lysine residues 82 beta interact with
2,3-diphosphoglycerate at the same time, each making two contacts. This level of
interaction is in agreement with the functional behaviour of natural haemoglobin
mutants with mutations at the 2,3-diphosphoglycerate binding site.
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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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M.Laberge,
and
T.Yonetani
(2008).
Molecular dynamics simulations of hemoglobin A in different states and bound to DPG: effector-linked perturbation of tertiary conformations and HbA concerted dynamics.
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Biophys J,
94,
2737-2751.
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D.Tobi,
and
I.Bahar
(2007).
Recruitment of rare 3-grams at functional sites: is this a mechanism for increasing enzyme specificity?
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BMC Bioinformatics,
8,
226.
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P.Nacharaju,
J.M.Friedman,
M.Prabhakaran,
S.A.Acharya,
and
B.N.Manjula
(2007).
Combining the influence of two low O2 affinity-inducing chemical modifications of the central cavity of hemoglobin.
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Biochemistry,
46,
4554-4564.
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S.Rezaei-Zarchi,
A.A.Saboury,
H.Ghourchian,
J.Hong,
A.Barzegar,
P.Norouzi,
A.A.Moosavi-Movahedi,
M.R.Ganjali,
and
A.Javed
(2007).
Electrochemical investigation of the effect of some organic phosphates on haemoglobin.
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J Biosci,
32,
271-278.
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C.J.Roche,
F.Guo,
and
J.M.Friedman
(2006).
Molecular level probing of preferential hydration and its modulation by osmolytes through the use of pyranine complexed to hemoglobin.
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J Biol Chem,
281,
38757-38768.
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L.N.Patskovska,
Y.V.Patskovsky,
S.C.Almo,
and
R.E.Hirsch
(2005).
COHbC and COHbS crystallize in the R2 quaternary state at neutral pH in the presence of PEG 4000.
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Acta Crystallogr D Biol Crystallogr,
61,
566-573.
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PDB codes:
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C.Verde,
V.Carratore,
A.Riccio,
M.Tamburrini,
E.Parisi,
and
G.Di Prisco
(2002).
The functionally distinct hemoglobins of the Arctic spotted wolffish Anarhichas minor.
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J Biol Chem,
277,
36312-36320.
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J.C.Dewan,
A.Feeling-Taylor,
Y.A.Puius,
L.Patskovska,
Y.Patskovsky,
R.L.Nagel,
S.C.Almo,
and
R.E.Hirsch
(2002).
Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A resolution.
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Acta Crystallogr D Biol Crystallogr,
58,
2038-2042.
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PDB code:
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M.K.Safo,
J.C.Burnett,
F.N.Musayev,
S.Nokuri,
and
D.J.Abraham
(2002).
Structure of human carbonmonoxyhemoglobin at 2.16 A: a snapshot of the allosteric transition.
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Acta Crystallogr D Biol Crystallogr,
58,
2031-2037.
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PDB code:
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A.Riccio,
M.Tamburrini,
B.Giardina,
and
G.di Prisco
(2001).
Molecular dynamics analysis of a second phosphate site in the hemoglobins of the seabird, south polar skua. Is there a site-site migratory mechanism along the central cavity?
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Biophys J,
81,
1938-1946.
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M.Pellegrini,
M.Corda,
L.Manca,
A.Olianas,
M.T.Sanna,
A.Fais,
M.C.De Rosa,
C.Bertonati,
B.Masala,
and
B.Giardina
(2001).
Functional and computer modelling studies of haemoglobin from horse. The haemoglobin system of the Sardinian wild dwarf horse.
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Eur J Biochem,
268,
3313-3320.
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R.E.Hirsch,
R.E.Samuel,
N.A.Fataliev,
M.J.Pollack,
O.Galkin,
P.G.Vekilov,
and
R.L.Nagel
(2001).
Differential pathways in oxy and deoxy HbC aggregation/crystallization.
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Proteins,
42,
99.
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H.C.Wang,
Y.H.Liang,
J.P.Zhu,
and
G.Y.Lu
(2000).
Crystallization and preliminary crystallographic studies of bar-headed goose fluoromethaemoglobin with inositol hexaphosphate.
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Acta Crystallogr D Biol Crystallogr,
56,
1183-1184.
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T.H.Lu,
K.Panneerselvam,
Y.C.Liaw,
P.Kan,
and
C.J.Lee
(2000).
Structure determination of porcine haemoglobin.
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Acta Crystallogr D Biol Crystallogr,
56,
304-312.
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PDB code:
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M.Coletta,
M.Angeletti,
I.Ascone,
G.Boumis,
A.C.Castellano,
M.Dell'Ariccia,
S.Della Longa,
G.De Sanctis,
A.M.Priori,
R.Santucci,
A.Feis,
and
G.Amiconi
(1999).
Heterotropic effectors exert more significant strain on monoligated than on unligated hemoglobin.
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Biophys J,
76,
1532-1536.
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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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Links
