1evr: Difference between revisions

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New page: left|200px<br /> <applet load="1evr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1evr, resolution 1.90Å" /> '''The structure of th...
 
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[[Image:1evr.gif|left|200px]]<br />
[[Image:1evr.gif|left|200px]]<br /><applet load="1evr" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1evr" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1evr, resolution 1.90&Aring;" />
caption="1evr, resolution 1.90&Aring;" />
'''The structure of the resorcinol/insulin R6 hexamer'''<br />
'''The structure of the resorcinol/insulin R6 hexamer'''<br />


==Overview==
==Overview==
The structures of three R(6) human insulin hexamers have been determined., Crystals of monoclinic m-cresol-insulin, monoclinic resorcinol-insulin and, rhombohedral m-cresol-insulin diffracted to 1. 9, 1.9 and 1.78 A, respectively, and have been refined to residuals of 0.195, 0.179 and, 0.200, respectively. In all three structures, a phenolic derivative is, found to occupy the phenolic binding site, where it forms hydrogen bonds, to the carbonyl O atom of CysA6 and the N atom of CysA11. Two additional, phenolic derivative binding sites were identified within or between, hexamers. The structures of all three hexamers are nearly identical, although a large displacement of the N-terminus of one B chain in both, monoclinic structures results from coordination to a sodium ion which is, located between symmetry-related hexamers. Other minor differences in, structure arise from differences in packing in the monoclinic cell, compared with the rhombohedral cell. Based upon the differences in, conformation of the GluB13 side chains in T(6), T(3)R(f)(3) and R(6), hexamers, the deprotonation of these side chains appears to be associated, with the T--&gt;R conformational transition.
The structures of three R(6) human insulin hexamers have been determined. Crystals of monoclinic m-cresol-insulin, monoclinic resorcinol-insulin and rhombohedral m-cresol-insulin diffracted to 1. 9, 1.9 and 1.78 A, respectively, and have been refined to residuals of 0.195, 0.179 and 0.200, respectively. In all three structures, a phenolic derivative is found to occupy the phenolic binding site, where it forms hydrogen bonds to the carbonyl O atom of CysA6 and the N atom of CysA11. Two additional phenolic derivative binding sites were identified within or between hexamers. The structures of all three hexamers are nearly identical, although a large displacement of the N-terminus of one B chain in both monoclinic structures results from coordination to a sodium ion which is located between symmetry-related hexamers. Other minor differences in structure arise from differences in packing in the monoclinic cell compared with the rhombohedral cell. Based upon the differences in conformation of the GluB13 side chains in T(6), T(3)R(f)(3) and R(6) hexamers, the deprotonation of these side chains appears to be associated with the T--&gt;R conformational transition.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1EVR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ZN, CL, NA and RCO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EVR OCA].  
1EVR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</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=1EVR OCA].  


==Reference==
==Reference==
R6 hexameric insulin complexed with m-cresol or resorcinol., Smith GD, Ciszak E, Magrum LA, Pangborn WA, Blessing RH, Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1541-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11092919 11092919]
R6 hexameric insulin complexed with m-cresol or resorcinol., Smith GD, Ciszak E, Magrum LA, Pangborn WA, Blessing RH, Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1541-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11092919 11092919]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Blessing, R.H.]]
[[Category: Blessing, R H.]]
[[Category: Ciszak, E.]]
[[Category: Ciszak, E.]]
[[Category: Magrum, L.A.]]
[[Category: Magrum, L A.]]
[[Category: Pangborn, W.A.]]
[[Category: Pangborn, W A.]]
[[Category: Smith, G.D.]]
[[Category: Smith, G D.]]
[[Category: CL]]
[[Category: CL]]
[[Category: NA]]
[[Category: NA]]
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[[Category: r6 insulin hexamer]]
[[Category: r6 insulin hexamer]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:46:59 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:01 2008''

Revision as of 13:32, 21 February 2008

File:1evr.gif


1evr, resolution 1.90Å

Drag the structure with the mouse to rotate

The structure of the resorcinol/insulin R6 hexamer

OverviewOverview

The structures of three R(6) human insulin hexamers have been determined. Crystals of monoclinic m-cresol-insulin, monoclinic resorcinol-insulin and rhombohedral m-cresol-insulin diffracted to 1. 9, 1.9 and 1.78 A, respectively, and have been refined to residuals of 0.195, 0.179 and 0.200, respectively. In all three structures, a phenolic derivative is found to occupy the phenolic binding site, where it forms hydrogen bonds to the carbonyl O atom of CysA6 and the N atom of CysA11. Two additional phenolic derivative binding sites were identified within or between hexamers. The structures of all three hexamers are nearly identical, although a large displacement of the N-terminus of one B chain in both monoclinic structures results from coordination to a sodium ion which is located between symmetry-related hexamers. Other minor differences in structure arise from differences in packing in the monoclinic cell compared with the rhombohedral cell. Based upon the differences in conformation of the GluB13 side chains in T(6), T(3)R(f)(3) and R(6) hexamers, the deprotonation of these side chains appears to be associated with the T-->R conformational transition.

DiseaseDisease

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

About this StructureAbout this Structure

1EVR is a Protein complex structure of sequences from [1] with , , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

R6 hexameric insulin complexed with m-cresol or resorcinol., Smith GD, Ciszak E, Magrum LA, Pangborn WA, Blessing RH, Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1541-8. PMID:11092919

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