1hre
From Proteopedia
(New page: 200px<br /> <applet load="1hre" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hre" /> '''SOLUTION STRUCTURE OF THE EPIDERMAL GROWTH ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1hre. | + | [[Image:1hre.jpg|left|200px]]<br /><applet load="1hre" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hre" size=" | + | |
caption="1hre" /> | caption="1hre" /> | ||
'''SOLUTION STRUCTURE OF THE EPIDERMAL GROWTH FACTOR-LIKE DOMAIN OF HEREGULIN-ALPHA, A LIGAND FOR P180ERB4'''<br /> | '''SOLUTION STRUCTURE OF THE EPIDERMAL GROWTH FACTOR-LIKE DOMAIN OF HEREGULIN-ALPHA, A LIGAND FOR P180ERB4'''<br /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1HRE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1HRE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRE OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 23: | ||
[[Category: growth factor]] | [[Category: growth factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:57:47 2008'' |
Revision as of 13:57, 15 February 2008
|
SOLUTION STRUCTURE OF THE EPIDERMAL GROWTH FACTOR-LIKE DOMAIN OF HEREGULIN-ALPHA, A LIGAND FOR P180ERB4
Contents |
Overview
p185erbB-2 and p180erbB-4 are epidermal growth factor (EGF) receptor-like, tyrosine kinases, whose co-expression is observed in many breast, carcinomas. Heregulins (HRGs), which contain an immunoglobulin unit and an, EGF-like domain, bind to p180erbB-4 and activate p180erbB-4 and p185erbB-2, through transphosphorylation or receptor heterodimerization. The EGF-like, domain is sufficient for the activation. Despite the sequence similarity, no cross activity is seen between the p180erbB-4 ligands (HRGs) and the, p170erbB-1 ligands [EGF and transforming growth factor (TGF)-alpha]. To, investigate the structural basis of receptor specificity, we have, determined the solution structure of the EGF-like domain of HRG-alpha by, two-dimensional 1H nuclear magnetic resonance spectroscopy and simulated, annealing calculations. Though its main-chain fold is similar to those of, EGF and TGF-alpha, distinctive structural features are observed on the, molecular surface including an ionic cluster and hydrophobic patches, which afford HRG-alpha the specific affinity for p180erbB-4. The structure, should provide a basis for the structure-activity relationship of HRGs and, for the design of drugs which prevent progression of breast cancer.
Disease
Known diseases associated with this structure: Fibromatosis, gingival, 2 OMIM:[605544], Schizophrenia, susceptibility to OMIM:[142445]
About this Structure
1HRE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erbB-4., Nagata K, Kohda D, Hatanaka H, Ichikawa S, Matsuda S, Yamamoto T, Suzuki A, Inagaki F, EMBO J. 1994 Aug 1;13(15):3517-23. PMID:8062828
Page seeded by OCA on Fri Feb 15 15:57:47 2008
