1sdb

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(New page: 200px<br /><applet load="1sdb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sdb, resolution 1.65&Aring;" /> '''PORCINE DESB1-2 DESP...)
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caption="1sdb, resolution 1.65&Aring;" />
caption="1sdb, resolution 1.65&Aring;" />
'''PORCINE DESB1-2 DESPENTAPEPTIDE(B26-B30) INSULIN'''<br />
'''PORCINE DESB1-2 DESPENTAPEPTIDE(B26-B30) INSULIN'''<br />
==Overview==
==Overview==
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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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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.
==About this Structure==
==About this Structure==
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1SDB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SDB OCA].
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1SDB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SDB OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Diao, J.S.]]
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[[Category: Diao, J S.]]
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[[Category: Liang, D.C.]]
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[[Category: Liang, D C.]]
[[Category: hormone]]
[[Category: hormone]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:17:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:21 2008''

Revision as of 13:00, 21 February 2008


1sdb, resolution 1.65Å

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PORCINE DESB1-2 DESPENTAPEPTIDE(B26-B30) INSULIN

Overview

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.

About this Structure

1SDB is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Structure of monomeric porcine DesB1-B2 despentapeptide (B26-B30) insulin at 1.65 A resolution., Diao JS, Wan ZL, Chang WR, Liang DC, Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):507-12. PMID:15299880

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