1pid

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1pid" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pid, resolution 1.3&Aring;" /> '''BOVINE DESPENTAPEPTID...)
Line 1: Line 1:
-
[[Image:1pid.gif|left|200px]]<br /><applet load="1pid" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1pid.gif|left|200px]]<br /><applet load="1pid" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pid, resolution 1.3&Aring;" />
caption="1pid, resolution 1.3&Aring;" />
'''BOVINE DESPENTAPEPTIDE INSULIN'''<br />
'''BOVINE DESPENTAPEPTIDE INSULIN'''<br />
==Overview==
==Overview==
-
The crystal structure of despentapeptide insulin, a monomeric insulin, has, been refined at 1.3 A spacing and subsequently used to predict and model, the organization in the insulin fibril. The model makes use of the, contacts in the densely packed despentapeptide insulin crystal, and takes, into account other experimental evidence, including binding studies with, Congo red. The dimensions of this model fibril correspond well with those, measured experimentally, and the monomer-monomer contacts within the, fibril are in accordance with the known physical chemistry of insulin, fibrils. Using this model, it may be possible to predict mutations in, insulin that might alleviate problems associated with fibril formation, during insulin therapy.
+
The crystal structure of despentapeptide insulin, a monomeric insulin, has been refined at 1.3 A spacing and subsequently used to predict and model the organization in the insulin fibril. The model makes use of the contacts in the densely packed despentapeptide insulin crystal, and takes into account other experimental evidence, including binding studies with Congo red. The dimensions of this model fibril correspond well with those measured experimentally, and the monomer-monomer contacts within the fibril are in accordance with the known physical chemistry of insulin fibrils. Using this model, it may be possible to predict mutations in insulin that might alleviate problems associated with fibril formation during insulin therapy.
==About this Structure==
==About this Structure==
-
1PID is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PID OCA].
+
1PID is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PID OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
-
[[Category: Dodson, G.G.]]
+
[[Category: Dodson, G G.]]
-
[[Category: Holden, P.H.]]
+
[[Category: Holden, P H.]]
[[Category: Papiz, M.]]
[[Category: Papiz, M.]]
[[Category: glucose metabolism]]
[[Category: glucose metabolism]]
[[Category: hormone]]
[[Category: hormone]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:50:11 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:05 2008''

Revision as of 12:29, 21 February 2008


1pid, resolution 1.3Å

Drag the structure with the mouse to rotate

BOVINE DESPENTAPEPTIDE INSULIN

Overview

The crystal structure of despentapeptide insulin, a monomeric insulin, has been refined at 1.3 A spacing and subsequently used to predict and model the organization in the insulin fibril. The model makes use of the contacts in the densely packed despentapeptide insulin crystal, and takes into account other experimental evidence, including binding studies with Congo red. The dimensions of this model fibril correspond well with those measured experimentally, and the monomer-monomer contacts within the fibril are in accordance with the known physical chemistry of insulin fibrils. Using this model, it may be possible to predict mutations in insulin that might alleviate problems associated with fibril formation during insulin therapy.

About this Structure

1PID is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

A model of insulin fibrils derived from the x-ray crystal structure of a monomeric insulin (despentapeptide insulin)., Brange J, Dodson GG, Edwards DJ, Holden PH, Whittingham JL, Proteins. 1997 Apr;27(4):507-16. PMID:9141131

Page seeded by OCA on Thu Feb 21 14:29:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools