1mso
From Proteopedia
(New page: 200px<br /> <applet load="1mso" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mso, resolution 1.00Å" /> '''T6 Human Insulin at...) |
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| - | [[Image:1mso.gif|left|200px]]<br /> | + | [[Image:1mso.gif|left|200px]]<br /><applet load="1mso" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1mso" size=" | + | |
caption="1mso, resolution 1.00Å" /> | caption="1mso, resolution 1.00Å" /> | ||
'''T6 Human Insulin at 1.0 A Resolution'''<br /> | '''T6 Human Insulin at 1.0 A Resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of T(6) human insulin has been determined at 120 K at a | + | The structure of T(6) human insulin has been determined at 120 K at a resolution of 1.0 A and refined to a residual of 0.183. As a result of cryofreezing, the first four residues of the B chain in one of the two crystallographically independent AB monomers in the hexameric [Zn(1/3)(AB)(2)Zn(1/3)](3) complex undergo a conformational shift that displaces the C(alpha) atom of PheB1 by 7.86 A relative to the room-temperature structure. A least-squares superposition of all backbone atoms of the room-temperature and low-temperature structures yielded a mean displacement of 0.422 A. Omitting the first four residues of the B chain reduced the mean displacement to 0.272 A. At 120 K, nine residues were found to exhibit two discrete side-chain conformations, but only two of these residues are in common with the seven residues found to have disordered side chains in the room-temperature structure. As a result of freezing, the disorder observed at room temperature in both ArgB22 side chains is eliminated. The close contact between pairs of O( epsilon 2) atoms in GluB13 observed at room temperature is maintained at cryotemperature and suggests that a carboxylate-carboxylic acid centered hydrogen bond exists [-C(=O)-O.H.O-C(=O)-] such that the H atom is equally shared between the two partially charged O atoms. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MSO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MSO 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MSO OCA]. |
==Reference== | ==Reference== | ||
The structure of T6 human insulin at 1.0 A resolution., Smith GD, Pangborn WA, Blessing RH, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):474-82. Epub 2003, Feb 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12595704 12595704] | The structure of T6 human insulin at 1.0 A resolution., Smith GD, Pangborn WA, Blessing RH, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):474-82. Epub 2003, Feb 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12595704 12595704] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Blessing, R | + | [[Category: Blessing, R H.]] |
| - | [[Category: Pangborn, W | + | [[Category: Pangborn, W A.]] |
| - | [[Category: Smith, G | + | [[Category: Smith, G D.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: t6 conformation]] | [[Category: t6 conformation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:37 2008'' |
Revision as of 11:58, 21 February 2008
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T6 Human Insulin at 1.0 A Resolution
Contents |
Overview
The structure of T(6) human insulin has been determined at 120 K at a resolution of 1.0 A and refined to a residual of 0.183. As a result of cryofreezing, the first four residues of the B chain in one of the two crystallographically independent AB monomers in the hexameric [Zn(1/3)(AB)(2)Zn(1/3)](3) complex undergo a conformational shift that displaces the C(alpha) atom of PheB1 by 7.86 A relative to the room-temperature structure. A least-squares superposition of all backbone atoms of the room-temperature and low-temperature structures yielded a mean displacement of 0.422 A. Omitting the first four residues of the B chain reduced the mean displacement to 0.272 A. At 120 K, nine residues were found to exhibit two discrete side-chain conformations, but only two of these residues are in common with the seven residues found to have disordered side chains in the room-temperature structure. As a result of freezing, the disorder observed at room temperature in both ArgB22 side chains is eliminated. The close contact between pairs of O( epsilon 2) atoms in GluB13 observed at room temperature is maintained at cryotemperature and suggests that a carboxylate-carboxylic acid centered hydrogen bond exists [-C(=O)-O.H.O-C(=O)-] such that the H atom is equally shared between the two partially charged O atoms.
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
1MSO is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
The structure of T6 human insulin at 1.0 A resolution., Smith GD, Pangborn WA, Blessing RH, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):474-82. Epub 2003, Feb 21. PMID:12595704
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