1k36

NMR Structure of human Epiregulin

spinqualitylabelsall models 1k36 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1k36 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 40 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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