| Autor: |
Andreeva NS, Fedorov AA, Gushchina AE, Riskulov RR, Shutskever NE, Safro MG |
| Jazyk: |
ruština |
| Zdroj: |
Molekuliarnaia biologiia [Mol Biol (Mosk)] 1978 Jul-Aug; Vol. 12 (4), pp. 922-36. |
| Abstrakt: |
A detailed description of structural investigations of pepsin from 3.5 to 2.7 A resolution are given. The main attention is drawn to the conformation of the polypeptide backbone of the enzyme. The numbers of amino acid residues involved in the formation of various structural elements are listed. The structure of pepsin is similar to that of acid proteases isolated from lower organisms. The two domain structure of all acid proteases has a periodicity in the sequence of beta-segments and helices and a very specific symmetrical structure of each domain. This makes it possible to describe the structure of acid proteases in simple terms. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
