2omi

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[[Image:2omi.gif|left|200px]]<br /><applet load="2omi" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2omi.gif|left|200px]]
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caption="2omi, resolution 2.24&Aring;" />
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'''Structure of human insulin cocrystallized with protamine'''<br />
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{{Structure
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|PDB= 2omi |SIZE=350|CAPTION= <scene name='initialview01'>2omi</scene>, resolution 2.24&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=RCO:RESORCINOL'>RCO</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Structure of human insulin cocrystallized with protamine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2OMI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=RCO:'>RCO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OMI OCA].
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2OMI is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OMI OCA].
==Reference==
==Reference==
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Structural characterization of insulin NPH formulations., Norrman M, Hubalek F, Schluckebier G, Eur J Pharm Sci. 2007 Apr;30(5):414-23. Epub 2007 Jan 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17339105 17339105]
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Structural characterization of insulin NPH formulations., Norrman M, Hubalek F, Schluckebier G, Eur J Pharm Sci. 2007 Apr;30(5):414-23. Epub 2007 Jan 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17339105 17339105]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: RCO]]
[[Category: RCO]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: insulin nph microcrystals]]
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[[Category: insulin nph microcrystal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:20:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:01:39 2008''

Revision as of 16:01, 20 March 2008


PDB ID 2omi

Drag the structure with the mouse to rotate
, resolution 2.24Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



Structure of human insulin cocrystallized with protamine


Contents

Overview

Insulin NPH (neutral protamine hagedorn) has for long been one of the most important therapeutic formulations for the treatment of diabetes. The protracted action profile of NPH formulations is gained from crystallizing insulin with zinc in the presence of the basic poly-arginine peptide protamine. In spite of its long history and successful use, the binding mode of the insulin-protamine complex is not known. In this study, three different systems were used to study protamine binding to insulin. In the first system, crystals of an insulin-protamine complex grown in the presence of urea and diffracting to 1.5A resolution were analyzed. In the second system, a shorter peptide consisting of 12 arginine residues was co-crystallized with insulin in order to reduce the flexibility and thereby improve the electron density of the peptide. Both systems yielded data to a significantly higher resolution than obtained previously. In addition, a third system was analyzed where crystals of insulin and protamine were grown in the absence of urea, with conditions closely resembling the pharmaceutical formulation. Data from these NPH microcrystals could for the first time be collected to 2.2A resolution at a micro focused X-ray beamline. Analysis of all three crystal forms reveal potential protamine density located close to the solvent channel leading to the centrally located zinc atoms in the insulin hexamer and support that protamine binds to insulin in a not well defined conformation.

Disease

Known diseases associated with this structure: Diabetes mellitus, rare form OMIM:[176730], Hyperproinsulinemia, familial OMIM:[176730], MODY, one form OMIM:[176730]

About this Structure

2OMI is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural characterization of insulin NPH formulations., Norrman M, Hubalek F, Schluckebier G, Eur J Pharm Sci. 2007 Apr;30(5):414-23. Epub 2007 Jan 20. PMID:17339105

Page seeded by OCA on Thu Mar 20 18:01:39 2008

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