𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Conformational and receptor binding properties of human EGF and TGF-α second loop fragments

✍ Scribed by Kyou-Hoon Han; James A. Ferretti; Chien-Hua Niu; Vinatu Lokeshwar; Robert Clarke; Deborah Katz

Book ID
102906084
Publisher
John Wiley and Sons
Year
1988
Tongue
English
Weight
828 KB
Volume
1
Category
Article
ISSN
0952-3499

No coin nor oath required. For personal study only.

✦ Synopsis

The solution conformation of the second loop fragment of human EGF, [Ala20] EGF (14-31), was determined using two-dimensional NMR homonuclear Hartmann-Hahn and rotating frame nuclear Overhauser enhancement spectroscopy. The results are compared with the conformation of the second loop fragment of human TGF-alpha, [Ala21] TGF-alpha(16-32), and with that of the second loop of intact EGF. Comparison of the two experimentally determined structures of the second loop fragments shows significant differences in the turn regions of each peptide. For the EGF fragment, hydrophobic side chain groups protrude away from the ring, whereas for the TGF-alpha fragment hydrophilic groups are directed away from the ring. Although these turn regions represent the putative receptor binding sites, neither second loop fragment binds to the EGF receptor. The biological activity is discussed in terms of the conformational differences found for the two second loop fragments.

📜 SIMILAR VOLUMES

Expression of TGF-α/EGF and TGF-p recept
Expression of TGF-α/EGF and TGF-p receptors in human colon carcinoma cell lines
✍ Uma Murthy; Mario A. Anzano; Russell G. Greig 📂 Article 📅 1989 🏛 John Wiley and Sons 🌐 French ⚖ 957 KB

Previous studies have established that colon carcinoma cells secrete several polypeptide growth factors, including TGF-dEGF and TGF-B, suggesting that these and related molecules function in an autocrindparacrine fashion to modulate tumor-cell growth. To investigate this possibility, we have studied

Human A673 cells secrete high molecular
Human A673 cells secrete high molecular weight EGF-receptor binding growth factors that appear to be immunologically unrelated to EGF or TGF-α
✍ Kurt Stromberg; W. Robert Hudgins; Charlotte M. Fryling; Parul Hazarika; John R. 📂 Article 📅 1986 🏛 John Wiley and Sons 🌐 English ⚖ 775 KB

Extracts of serum-free conditioned medium from human rhabdomyosarcoma A673 cells contain high molecular weight (HMW) transforming growth factors (TGFs) that can be partially purified by Bio-Gel P-100 and carboxymethyl (CM)-cellulose chromatography (Todaro et al: Proc Natl Acad Sci USA 775258, 1980).