1k36

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==NMR Structure of human Epiregulin==
==NMR Structure of human Epiregulin==
-
<StructureSection load='1k36' size='340' side='right'caption='[[1k36]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
+
<StructureSection load='1k36' size='340' side='right'caption='[[1k36]]' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1k36]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K36 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1k36]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K36 FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1k37|1k37]]</div></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1k36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k36 OCA], [https://pdbe.org/1k36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k36 RCSB], [https://www.ebi.ac.uk/pdbsum/1k36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k36 ProSAT]</span></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=1k36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k36 OCA], [https://pdbe.org/1k36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k36 RCSB], [https://www.ebi.ac.uk/pdbsum/1k36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k36 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/EREG_HUMAN EREG_HUMAN]] Ligand of the EGF receptor/EGFR and ERBB4. May be a mediator of localized cell proliferation. As a mitogen it may stimulate cell proliferation and/or angiogenesis.<ref>PMID:9419975</ref>
+
[https://www.uniprot.org/uniprot/EREG_HUMAN EREG_HUMAN] Ligand of the EGF receptor/EGFR and ERBB4. May be a mediator of localized cell proliferation. As a mitogen it may stimulate cell proliferation and/or angiogenesis.<ref>PMID:9419975</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 19:
</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=1k36 ConSurf].
</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=1k36 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR for the receptors is lower than those of other EGF-family ligands. The solution structure of EPR was determined using two-dimensional nuclear magnetic resonance spectroscopy. The secondary structure in the C-terminal domain of EPR is different from other EGF-family ligands because of the lack of hydrogen bonds. The structural difference in the C-terminal domain may provide an explanation for the reduced binding affinity of EPR to the ErbB receptors.
 
- 
-
Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity.,Sato K, Nakamura T, Mizuguchi M, Miura K, Tada M, Aizawa T, Gomi T, Miyamoto K, Kawano K FEBS Lett. 2003 Oct 23;553(3):232-8. PMID:14572630<ref>PMID:14572630</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 1k36" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Aizawa, T]]
+
[[Category: Aizawa T]]
-
[[Category: Kawano, K]]
+
[[Category: Kawano K]]
-
[[Category: Miura, K]]
+
[[Category: Miura K]]
-
[[Category: Miyamoto, K]]
+
[[Category: Miyamoto K]]
-
[[Category: Sato, K]]
+
[[Category: Sato K]]
-
[[Category: Tada, M]]
+
[[Category: Tada M]]
-
[[Category: Egf-like fold]]
+
-
[[Category: Hormone-growth factor complex]]
+

Revision as of 07:57, 3 April 2024

NMR Structure of human Epiregulin

PDB ID 1k36

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools