This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6ins
From Proteopedia
(Difference between revisions)
| (8 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:6ins.gif|left|200px]] | ||
| - | + | ==X-RAY ANALYSIS OF THE SINGLE CHAIN B29-A1 PEPTIDE-LINKED INSULIN MOLECULE. A COMPLETELY INACTIVE ANALOGUE== | |
| - | + | <StructureSection load='6ins' size='340' side='right' caption='[[6ins]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[6ins]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6INS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6INS FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | -- | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ins FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ins OCA], [http://pdbe.org/6ins PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ins RCSB], [http://www.ebi.ac.uk/pdbsum/6ins PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ins ProSAT]</span></td></tr> |
| - | + | </table> | |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/INS_PIG INS_PIG]] Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/in/6ins_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=6ins ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A crystal structure of a totally inactive insulin molecule has been determined. For this insulin molecule, the first without detectable activity to be characterized, the A and B-chains are linked by a peptide bond between A1 Gly and B29 Lys. The molecule has retained all its normal self-association properties and it can also accommodate the two different conformations designated T and R, as seen in 4Zn native pig insulin crystals. The hexamers of the crosslinked insulin molecule were crystallized using the 4Zn insulin recipe of Schlichtkrull. The structure has been crystallographically refined with data extending to 2 A using restrained least-square methods. Comparison of the B29-A1 peptide crosslink insulin and the 4Zn native insulin reveals close structural similarities with the native dimer. The analysis of the structure confirms the earlier hypothesis that insulin structures in crystals are not in an active conformation and that a separation of N-terminal A-chain and C-terminal B-chain is required for interaction with the insulin receptor. | ||
| - | + | X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue.,Derewenda U, Derewenda Z, Dodson EJ, Dodson GG, Bing X, Markussen J J Mol Biol. 1991 Jul 20;220(2):425-33. PMID:1856866<ref>PMID:1856866</ref> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 6ins" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Molecular Playground/Insulin|Molecular Playground/Insulin]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Bing, X | + | __TOC__ |
| - | [[Category: Derewenda, U | + | </StructureSection> |
| - | [[Category: Derewenda, Z | + | [[Category: Pig]] |
| - | [[Category: Dodson, E J | + | [[Category: Bing, X]] |
| - | [[Category: Dodson, G G | + | [[Category: Derewenda, U]] |
| - | [[Category: Markussen, J | + | [[Category: Derewenda, Z]] |
| + | [[Category: Dodson, E J]] | ||
| + | [[Category: Dodson, G G]] | ||
| + | [[Category: Markussen, J]] | ||
[[Category: Hormone]] | [[Category: Hormone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:41:28 2008'' | ||
Current revision
X-RAY ANALYSIS OF THE SINGLE CHAIN B29-A1 PEPTIDE-LINKED INSULIN MOLECULE. A COMPLETELY INACTIVE ANALOGUE
| |||||||||||
Categories: Pig | Bing, X | Derewenda, U | Derewenda, Z | Dodson, E J | Dodson, G G | Markussen, J | Hormone

