1md6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:00, 30 October 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1md6.gif|left|200px]]
 
-
{{Structure
+
==High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity==
-
|PDB= 1md6 |SIZE=350|CAPTION= <scene name='initialview01'>1md6</scene>, resolution 1.6&Aring;
+
<StructureSection load='1md6' size='340' side='right'caption='[[1md6]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[1md6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MD6 FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
-
|GENE=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1md6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1md6 OCA], [https://pdbe.org/1md6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1md6 RCSB], [https://www.ebi.ac.uk/pdbsum/1md6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1md6 ProSAT]</span></td></tr>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1md6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1md6 OCA], [http://www.ebi.ac.uk/pdbsum/1md6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1md6 RCSB]</span>
+
[https://www.uniprot.org/uniprot/I36RA_MOUSE I36RA_MOUSE] Is a highly and a specific antagonist of the IL-1 receptor-related protein 2-mediated response to interleukin 1 family member 9 (IL1F9). Could constitute part of an independent signaling system analogous to interleukin-1 alpha (IL-1A), beta (IL-1B) receptor agonist and interleukin-1 receptor type I (IL-1R1), that is present in epithelial barriers and takes part in local inflammatory response (By similarity).
-
}}
+
== 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/md/1md6_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1md6 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Interleukin-1 (IL-1) F5 is a novel member of the IL-1 family. The IL-1 family are involved in innate immune responses to infection and injury. These cytokines bind to specific receptors and cause activation of NFkappaB and MAP kinase. IL-1F5 has a sequence identity of 44% to IL-1 receptor antagonist (IL-1Ra), a natural antagonist of the IL-1 system. Here we report the crystal structure of IL-1F5 to a resolution of 1.6 A. It has the same beta-trefoil fold as other IL-1 family members, and the hydrophobic core is well conserved. However, there are substantial differences in the loop conformations, structures that confer binding specificity for the cognate receptor to IL-1beta and the antagonist IL-1Ra. Docking and superimposition of the IL-1F5 structure suggest that is unlikely to bind to the interleukin1 receptor, consistent with biochemical studies. The structure IL-1F5 lacks features that confer antagonist properties on IL-1Ra, and we predict that like IL-1beta it will act as an agonist. These studies give insights into how distinct receptor specificities can evolve within related cytokine families.
-
'''High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity'''
+
High-resolution structure of murine interleukin 1 homologue IL-1F5 reveals unique loop conformations for receptor binding specificity.,Dunn EF, Gay NJ, Bristow AF, Gearing DP, O'Neill LA, Pei XY Biochemistry. 2003 Sep 23;42(37):10938-44. PMID:12974628<ref>PMID:12974628</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1md6" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
Interleukin-1 (IL-1) F5 is a novel member of the IL-1 family. The IL-1 family are involved in innate immune responses to infection and injury. These cytokines bind to specific receptors and cause activation of NFkappaB and MAP kinase. IL-1F5 has a sequence identity of 44% to IL-1 receptor antagonist (IL-1Ra), a natural antagonist of the IL-1 system. Here we report the crystal structure of IL-1F5 to a resolution of 1.6 A. It has the same beta-trefoil fold as other IL-1 family members, and the hydrophobic core is well conserved. However, there are substantial differences in the loop conformations, structures that confer binding specificity for the cognate receptor to IL-1beta and the antagonist IL-1Ra. Docking and superimposition of the IL-1F5 structure suggest that is unlikely to bind to the interleukin1 receptor, consistent with biochemical studies. The structure IL-1F5 lacks features that confer antagonist properties on IL-1Ra, and we predict that like IL-1beta it will act as an agonist. These studies give insights into how distinct receptor specificities can evolve within related cytokine families.
+
*[[Interleukin 3D structures|Interleukin 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1MD6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MD6 OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
High-resolution structure of murine interleukin 1 homologue IL-1F5 reveals unique loop conformations for receptor binding specificity., Dunn EF, Gay NJ, Bristow AF, Gearing DP, O'Neill LA, Pei XY, Biochemistry. 2003 Sep 23;42(37):10938-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12974628 12974628]
+
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Single protein]]
+
[[Category: Dunn EF]]
-
[[Category: Dunn, E F.]]
+
[[Category: Gay NJ]]
-
[[Category: Gay, N J.]]
+
[[Category: O'Neill LA]]
-
[[Category: Neill, L A.O.]]
+
[[Category: Pei XY]]
-
[[Category: Pei, X Y.]]
+
-
[[Category: alpha helix]]
+
-
[[Category: beta triple]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:14:37 2008''
+

Current revision

High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity

PDB ID 1md6

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1md6"
Personal tools