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PDBsum entry 1spp
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Complex (seminal plasma protein/spp)
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PDB id
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1spp
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The crystal structures of two spermadhesins reveal the cub domain fold.
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Authors
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A.Romero,
M.J.Romão,
P.F.Varela,
I.Kölln,
J.M.Dias,
A.L.Carvalho,
L.Sanz,
E.Töpfer-Petersen,
J.J.Calvete.
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Ref.
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Nat Struct Biol, 1997,
4,
783-788.
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PubMed id
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Abstract
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Spermadhesins, 12,000-14,000 M(r) mammalian proteins, include lectins involved
in sperm-egg binding and display a single CUB domain architecture. We report the
crystal structures of porcine seminal plasma PSP-I/PSP-II, a heterodimer of two
glycosylated spermadhesins, and bovine aSFP at 2.4 A and 1.9 A resolution
respectively.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray diffraction analysis of boar seminal plasma spermadhesin psp-I/psp-Ii, A heterodimer of two cub domains.
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Authors
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A.Romero,
P.F.Varela,
L.Sanz,
E.Töpfer-Petersen,
J.J.Calvete.
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Ref.
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FEBS Lett, 1996,
382,
15-17.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. (A) Hexagonal crystal of the PSP-I/PSP-II heterodimer com-
plex grown in 30% polyethylene glycol 2000, 0.1 M ammonium
acetate, pH 6.5, at an estimated final protein concentration of 15
mg/ml. size is 0.5×0.2×0.2 mm a. (B) Trigonal crystal ob-
tained with the same crystallization buffer, but with a final protein
of about 37.5 mg/ml. The crystal size is 0.8×0.4×0.4
mm 3.
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The above figure is
reproduced from the cited reference
with permission from the Federation of European Biochemical Societies
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Secondary reference #2
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Title
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Boar spermadhesin psp-Ii: location of posttranslational modifications, Heterodimer formation with psp-I glycoforms and effect of dimerization on the ligand-Binding capabilities of the subunits.
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Authors
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J.J.Calvete,
K.Mann,
W.Schäfer,
M.Raida,
L.Sanz,
E.Töpfer-Petersen.
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Ref.
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Febs Lett, 1995,
365,
179-182.
[DOI no: ]
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PubMed id
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Figure 2.
Fig. 2. Alignment of the amino acid sequences of spermadhesins. Positions with absolutely conserved residues ( ) and conservative substitutions (,)
in all polypeptides are shown N 5°, asparagine residues which are constitutively glycosylated in (8) and in glycoforms of AQN-3 (8) and
AWN (12,13); N 98, glycosylated asparagine in PSP-II (this work); S 5 an T 95 serine and threonine residues which are O-glycosylated in glycoforms
of AWN (13).
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Figure 3.
Fig. 3. Fractionation of the non-heparin-binding fraction of boar sem-
inal plasma by gel filtration on Sephadex G-50. The elution position of
molecular mass standards is indicated at the top: DB, dextran blue 2000
(< 2,000 kDa); BSA, bovine serum albumin (67 kDa); OVA, ovalbumin
(43 kDa); RIB, A (14 kDa); COB, cyanocobalamine (1,350
Da). The symbol 'o' along the PSP-I/PSP-II peak (...) indicates the
elution osition of samples which were analyzed by reverse-phase
HPLC (as in Fig. 1) followed by quanitation of isolated PSP-I and
PSP-II by amino acid analysis. The discontinous line shows the eluting
position of isolated PSP-I and PSP-II.
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The above figures are
reproduced from the cited reference
with permission from the Federation of European Biochemical Societies
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Secondary reference #3
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Title
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The cub domain. A widespread module in developmentally regulated proteins.
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Authors
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P.Bork,
G.Beckmann.
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Ref.
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J Mol Biol, 1993,
231,
539-545.
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PubMed id
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