2int
From Proteopedia
(Difference between revisions)
| (15 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2int.gif|left|200px]]<br /><applet load="2int" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2int, resolution 2.35Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4'''<br /> | ||
| - | == | + | ==CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4== |
| + | <StructureSection load='2int' size='340' side='right'caption='[[2int]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2int]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2INT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2INT FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2int FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2int OCA], [https://pdbe.org/2int PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2int RCSB], [https://www.ebi.ac.uk/pdbsum/2int PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2int ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[https://www.uniprot.org/uniprot/IL4_HUMAN IL4_HUMAN]] Genetic variations in IL4 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[https://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:14681304</ref> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/IL4_HUMAN IL4_HUMAN]] Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. | ||
| + | == 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/2int_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=2int ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The crystal structure of recombinant human interleukin-4 (rhuIL-4) was initially determined at 3.5-A resolution by multiple isomorphous replacement techniques and subsequently refined to a resolution of 2.35 A by simulated annealing. The final crystallographic R-factor, based on all data in the range 6.0-2.35 A (7470 reflections), is 0.232. Bond lengths and bond angles in the molecule have root mean square deviations from ideal values of 0.016 A and 2.4 degrees, respectively. The overall structure is highly compact and globular with a predominantly hydrophobic core. The main structural feature of rhuIL-4 is a four alpha-helix bundle, which composes approximately 58% of the structure. The helices are arranged in a left-handed antiparallel bundle with two overhand connections. Within these connections is a two-stranded antiparallel beta-sheet. Both the tertiary and secondary structures of rhuIL-4 are similar to those of human granulocyte-macrophage colony-stimulating factor. Critical regions for receptor binding are proposed. | The crystal structure of recombinant human interleukin-4 (rhuIL-4) was initially determined at 3.5-A resolution by multiple isomorphous replacement techniques and subsequently refined to a resolution of 2.35 A by simulated annealing. The final crystallographic R-factor, based on all data in the range 6.0-2.35 A (7470 reflections), is 0.232. Bond lengths and bond angles in the molecule have root mean square deviations from ideal values of 0.016 A and 2.4 degrees, respectively. The overall structure is highly compact and globular with a predominantly hydrophobic core. The main structural feature of rhuIL-4 is a four alpha-helix bundle, which composes approximately 58% of the structure. The helices are arranged in a left-handed antiparallel bundle with two overhand connections. Within these connections is a two-stranded antiparallel beta-sheet. Both the tertiary and secondary structures of rhuIL-4 are similar to those of human granulocyte-macrophage colony-stimulating factor. Critical regions for receptor binding are proposed. | ||
| - | + | Crystal structure of recombinant human interleukin-4.,Walter MR, Cook WJ, Zhao BG, Cameron RP Jr, Ealick SE, Walter RL Jr, Reichert P, Nagabhushan TL, Trotta PP, Bugg CE J Biol Chem. 1992 Oct 5;267(28):20371-6. PMID:1400355<ref>PMID:1400355</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2int" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Interleukin 3D structures|Interleukin 3D structures]] | |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Bugg, C E | + | __TOC__ |
| - | [[Category: Cook, W J | + | </StructureSection> |
| - | [[Category: Ealick, S E | + | [[Category: Human]] |
| - | [[Category: Junior, R Cameron | + | [[Category: Large Structures]] |
| - | [[Category: Junior, R L.Walter | + | [[Category: Bugg, C E]] |
| - | [[Category: Nagabhushan, T L | + | [[Category: Cook, W J]] |
| - | [[Category: Reichert, P | + | [[Category: Ealick, S E]] |
| - | [[Category: Trotta, P P | + | [[Category: Junior, R Cameron]] |
| - | [[Category: Walter, M R | + | [[Category: Junior, R L.Walter]] |
| - | [[Category: Zhao, B G | + | [[Category: Nagabhushan, T L]] |
| - | [[Category: | + | [[Category: Reichert, P]] |
| - | + | [[Category: Trotta, P P]] | |
| - | + | [[Category: Walter, M R]] | |
| + | [[Category: Zhao, B G]] | ||
| + | [[Category: Cytokine]] | ||
Current revision
CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4
| |||||||||||
