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Lactose synthase
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PDB id
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1a4v
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Contents |
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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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2 terms
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Biological process
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cell-cell signaling
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5 terms
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Biochemical function
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protein binding
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3 terms
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DOI no:
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Biochemistry
37:4767-4772
(1998)
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PubMed id:
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Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin.
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N.Chandra,
K.Brew,
K.R.Acharya.
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ABSTRACT
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The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8
A) in the presence of an elevated level of calcium reveals a new secondary
calcium binding site, 7.9 A away from the primary calcium binding site known in
all alpha-lactalbumin structures so far. The new calcium binding site is
different from the zinc and sulfate binding sites [Ren, J., et al. (1993) J.
but shares common features with the manganese
binding site as described by Gerkin [Gerkin, T. A. (1984) Biochemistry 23,
4688-4697]. The proximity of the manganese and calcium binding region and the
location of the functional site on one side of the charged surface of the
alpha-lactalbumin molecule suggest that these binding sites might play a role in
the formation of the lactose synthase complex.
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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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J.A.Doebbler,
and
R.B.Von Dreele
(2009).
Application of molecular replacement to protein powder data from image plates.
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Acta Crystallogr D Biol Crystallogr, 65,
348-355.
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L.Gustafsson,
S.Aits,
P.Onnerfjord,
M.Trulsson,
P.Storm,
and
C.Svanborg
(2009).
Changes in proteasome structure and function caused by HAMLET in tumor cells.
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PLoS ONE, 4,
e5229.
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A.A.Thoppil,
and
N.Kishore
(2007).
Equimolar mixture of 2,2,2-trifluoroethanol and 4-chloro-1-butanol is a stronger inducer of molten globule state: isothermal titration calorimetric and spectroscopic studies.
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Protein J, 26,
507-516.
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G.van den Bogaart,
V.Krasnikov,
and
B.Poolman
(2007).
Dual-color fluorescence-burst analysis to probe protein efflux through the mechanosensitive channel MscL.
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Biophys J, 92,
1233-1240.
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M.Nakamura,
A.Takamizawa,
H.Yamada,
K.Hiraoka,
and
S.Akashi
(2007).
Denaturation of alpha-lactalbumin and ubiquitin studied by electrospray and laser spray.
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Rapid Commun Mass Spectrom, 21,
1635-1643.
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J.Wirmer,
H.Berk,
R.Ugolini,
C.Redfield,
and
H.Schwalbe
(2006).
Characterization of the unfolded state of bovine alpha-lactalbumin and comparison with unfolded states of homologous proteins.
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Protein Sci, 15,
1397-1407.
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S.E.Permyakov,
T.I.Khokhlova,
A.A.Nazipova,
A.P.Zhadan,
L.A.Morozova-Roche,
and
E.A.Permyakov
(2006).
Calcium-binding and temperature induced transitions in equine lysozyme: new insights from the pCa-temperature "phase diagrams".
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Proteins, 65,
984-998.
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T.K.Chaudhuri,
M.Arai,
T.P.Terada,
T.Ikura,
and
K.Kuwajima
(2000).
Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human alpha-lactalbumin by circular dichroism spectroscopy.
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Biochemistry, 39,
15643-15651.
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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.
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Links
