PANCREATIC SPASMOLYTIC POLYPEPTIDE - FIRST 3-DIMENSIONAL STRUCTURE OF A MEMBER OF THE MAMMALIAN TREFOIL FAMILY OF PEPTIDES

被引：65

作者：

GAJHEDE, M

PETERSEN, TN

HENRIKSEN, A

PETERSEN, JFW

DAUTER, Z

WILSON, KS

THIM, L

机构：

[1] DESY,EUROPEAN MOLEC BIOL LAB,D-22603 HAMBURG,GERMANY

[2] NOVO NORDISK AS,DK-2880 BAGSVAERD,DENMARK

来源：

STRUCTURE | 1993年 / 1卷 / 04期

关键词：

MUCUS LAYER; P-DOMAIN; PANCREATIC SPASMOLYTIC POLYPEPTIDE; TREFOIL FAMILY; X-RAY STRUCTURE;

D O I：

10.1016/0969-2126(93)90014-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Background: The trefoil peptides are a rapidly grow ing family of peptides, mainly found in the gastrointestinal tract. There is circumstantial evidence that they stabilize the mucus layer, and may affect the rate of healing of the mucosal epithelium. Results: We have determined the structure of porcine pancreatic spasmolytic polypeptide (PSP) to 2.5 Angstrom resolution. The polypeptide contains two trefoil domains. The domain structure is compact, and is composed of a central short antiparallel beta-sheet with one short helix above and one below it. This is a novel motif. The two domains are related by two-fold symmetry, and each domain contains a cleft. Conclusions: The cleft within each domain could accommodate a polysaccharide chain, and may therefore be responsible for binding mucin glycoproteins. We suggest that PSP may cross-link glycoproteins, explain ing its ability to stabilize the mucus layer.

引用

页码：253 / 262

页数：10

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