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PDBsum entry 2dg2
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Protein binding
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PDB id
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2dg2
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Protein binding
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Title:
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Crystal structure of mouse apolipoprotein a-i binding protein
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Structure:
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Apolipoprotein a-i binding protein. Chain: a, b, c, d, e, f. Fragment: residues 0-264. Engineered: yes
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Gene: apoa1bp. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
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Resolution:
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2.45Å
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R-factor:
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0.207
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R-free:
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0.228
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Authors:
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I.A.Shumilin,K.N.Jha,H.Zheng,M.Chruszcz,M.Cymborowski,J.C.Herr, W.Minor
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Key ref:
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K.N.Jha
et al.
(2008).
Biochemical and structural characterization of apolipoprotein A-I binding protein, a novel phosphoprotein with a potential role in sperm capacitation.
Endocrinology,
149,
2108-2120.
PubMed id:
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Date:
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08-Mar-06
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Release date:
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27-Mar-07
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PROCHECK
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Headers
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References
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Q8K4Z3
(NNRE_MOUSE) -
NAD(P)H-hydrate epimerase from Mus musculus
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Seq:
Struc:
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282 a.a.
233 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.5.1.99.6
- NAD(P)H-hydrate epimerase.
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Reaction:
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1.
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(6R)-NADHX = (6S)-NADHX
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2.
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(6R)-NADPHX = (6S)-NADPHX
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Endocrinology
149:2108-2120
(2008)
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PubMed id:
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Biochemical and structural characterization of apolipoprotein A-I binding protein, a novel phosphoprotein with a potential role in sperm capacitation.
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K.N.Jha,
I.A.Shumilin,
L.C.Digilio,
O.Chertihin,
H.Zheng,
G.Schmitz,
P.E.Visconti,
C.J.Flickinger,
W.Minor,
J.C.Herr.
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ABSTRACT
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The physiological changes that sperm undergo in the female reproductive tract
rendering them fertilization-competent constitute the phenomenon of
capacitation. Cholesterol efflux from the sperm surface and protein kinase A
(PKA)-dependent phosphorylation play major regulatory roles in capacitation, but
the link between these two phenomena is unknown. We report that apolipoprotein
A-I binding protein (AI-BP) is phosphorylated downstream to PKA activation,
localizes to both sperm head and tail domains, and is released from the sperm
into the media during in vitro capacitation. AI-BP interacts with apolipoprotein
A-I, the component of high-density lipoprotein involved in cholesterol
transport. The crystal structure demonstrates that the subunit of the AI-BP
homodimer has a Rossmann-like fold. The protein surface has a large two
compartment cavity lined with conserved residues. This cavity is likely to
constitute an active site, suggesting that AI-BP functions as an enzyme. The
presence of AI-BP in sperm, its phosphorylation by PKA, and its release during
capacitation suggest that AI-BP plays an important role in capacitation possibly
providing a link between protein phosphorylation and cholesterol efflux.
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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.L.Marshall,
D.L.Huestis,
C.Garcia,
Y.Hiromasa,
S.Wheeler,
S.Noh,
J.M.Tomich,
and
D.J.Howard
(2011).
Comparative proteomics uncovers the signature of natural selection acting on the ejaculate proteomes of two cricket species isolated by postmating, prezygotic phenotypes.
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Mol Biol Evol,
28,
423-435.
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A.Asano,
J.L.Nelson,
S.Zhang,
and
A.J.Travis
(2010).
Characterization of the proteomes associating with three distinct membrane raft sub-types in murine sperm.
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Proteomics,
10,
3494-3505.
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C.L.Borg,
K.M.Wolski,
G.M.Gibbs,
and
M.K.O'Bryan
(2010).
Phenotyping male infertility in the mouse: how to get the most out of a 'non-performer'.
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Hum Reprod Update,
16,
205-224.
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S.Singh
(2010).
Recent advances in physiological priming of spermatozoa.
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J Hum Reprod Sci,
3,
163-164.
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P.Bernthaler,
K.Epping,
G.Schmitz,
P.Deplazes,
and
K.Brehm
(2009).
Molecular characterization of EmABP, an apolipoprotein A-I binding protein secreted by the Echinococcus multilocularis metacestode.
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Infect Immun,
77,
5564-5571.
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S.D.Horswell,
H.E.Ringham,
and
C.C.Shoulders
(2009).
New technologies for delineating and characterizing the lipid exome: prospects for understanding familial combined hyperlipidemia.
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J Lipid Res,
50,
S370-S375.
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S.H.Ling,
C.J.Decker,
M.A.Walsh,
M.She,
R.Parker,
and
H.Song
(2008).
Crystal structure of human Edc3 and its functional implications.
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Mol Cell Biol,
28,
5965-5976.
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PDB codes:
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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
