1htv: Difference between revisions

New page: left|200px<br /> <applet load="1htv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1htv, resolution 1.90Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1htv.gif|left|200px]]<br />
[[Image:1htv.gif|left|200px]]<br /><applet load="1htv" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1htv" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1htv, resolution 1.90&Aring;" />
caption="1htv, resolution 1.90&Aring;" />
'''CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN'''<br />
'''CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN'''<br />


==Overview==
==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.
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==
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].  
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]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:22:26 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:47 2008''

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