1htv

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(New page: 200px<br /> <applet load="1htv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1htv, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE O...)
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'''CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN'''<br />
'''CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN'''<br />
==Overview==
==Overview==
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Destripeptide (B28-B30) insulin (DTRI) is an insulin analogue that has, much weaker association ability than native insulin but keeps most of its, biological activity. It can be crystallized from a solution containing, zinc ions at near-neutral pH. Its crystal structure has been determined by, molecular replacement and refined at 1.9 A resolution. DTRI in the crystal, exists as a loose hexamer compared with 2Zn insulin. The hexamer only, contains one zinc ion that coordinates to the B10 His residues of three, monomers. Although residues B28-B30 are located in the monomer-monomer, interface within a dimer, the removal of them can simultaneously weaken, both the interactions between monomers within the dimer and the, interactions between dimers. Because the B-chain C-terminus of insulin is, very flexible, we take the DTRI hexamer as a transition state in the, native insulin dissociation process and suggest a possible dissociation, process of the insulin hexamer based on the DTRI structure.
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Destripeptide (B28-B30) insulin (DTRI) is an insulin analogue that has much weaker association ability than native insulin but keeps most of its biological activity. It can be crystallized from a solution containing zinc ions at near-neutral pH. Its crystal structure has been determined by molecular replacement and refined at 1.9 A resolution. DTRI in the crystal exists as a loose hexamer compared with 2Zn insulin. The hexamer only contains one zinc ion that coordinates to the B10 His residues of three monomers. Although residues B28-B30 are located in the monomer-monomer interface within a dimer, the removal of them can simultaneously weaken both the interactions between monomers within the dimer and the interactions between dimers. Because the B-chain C-terminus of insulin is very flexible, we take the DTRI hexamer as a transition state in the native insulin dissociation process and suggest a possible dissociation process of the insulin hexamer based on the DTRI structure.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1HTV 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 ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HTV OCA].
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1HTV 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTV OCA].
==Reference==
==Reference==
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[[Category: helix]]
[[Category: helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:22:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:47 2008''

Revision as of 11:04, 21 February 2008

Image:1htv.gif

1htv, resolution 1.90Å

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CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN

Contents

Overview

Destripeptide (B28-B30) insulin (DTRI) is an insulin analogue that has much weaker association ability than native insulin but keeps most of its biological activity. It can be crystallized from a solution containing zinc ions at near-neutral pH. Its crystal structure has been determined by molecular replacement and refined at 1.9 A resolution. DTRI in the crystal exists as a loose hexamer compared with 2Zn insulin. The hexamer only contains one zinc ion that coordinates to the B10 His residues of three monomers. Although residues B28-B30 are located in the monomer-monomer interface within a dimer, the removal of them can simultaneously weaken both the interactions between monomers within the dimer and the interactions between dimers. Because the B-chain C-terminus of insulin is very flexible, we take the DTRI hexamer as a transition state in the native insulin dissociation process and suggest a possible dissociation process of the insulin hexamer based on the DTRI structure.

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

1HTV is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of destripeptide (B28-B30) insulin: implications for insulin dissociation., Ye J, Chang W, Liang D, Biochim Biophys Acta. 2001 May 5;1547(1):18-25. PMID:11343787

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