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PDBsum entry 1sdb
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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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Structure of monomeric porcine desb1-B2 despentapeptide (b26-B30) insulin at 1.65 a resolution.
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Authors
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J.S.Diao,
Z.L.Wan,
W.R.Chang,
D.C.Liang.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1997,
53,
507-512.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
88%.
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Abstract
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Insulin has a concentration of 10(-8)-10(-11) M in the blood which ensures that
it circulates and exerts its physiological functions in vivo as a monomer. The
crystal structure of monomeric porcine desB1-B2 despentapeptide (B26-B30)
insulin (DesB1-2 DPI) with M(r) = 4934 Da has been determined at 1.65 A
resolution using the molecular replacement method. A structural comparison
between DesB1-2 DPI and 2Zn insulin reveals that the conformation of DesB1-2 DPI
is more similar to molecule I than molecule II of 2Zn insulin. The remarkable
conformational difference between B25-Phe in DesB1-2 DPI and B25-Phe in
despentapeptide (B26-B30) insulin (DPI) indicates that the residue B25-Phe
possesses great flexibility and mobility.
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Figure 2.
Fig. 2. Stereoview of residue A19
Tyr superimposed with the corre
sponding F o F~ map contoured
at 2.0o.
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Figure 4.
Fig. 4. Stereoview of the F o F~
omit map of residues B23B25
contoured at 2.0o.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1997,
53,
507-512)
copyright 1997.
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Secondary reference #1
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Title
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Refinement of the structure of despentapeptide (b26-B30) insulin at 1.5a resolution
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Authors
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J.B.Dai,
M.Z.Lou,
J.M.You,
D.C.Liang.
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Ref.
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sci sin (engl ed ), 1987,
30,
55.
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