H-1 NMR-BASED DETERMINATION OF THE SECONDARY STRUCTURE OF PORCINE PANCREATIC SPASMOLYTIC POLYPEPTIDE - ONE OF A NEW FAMILY OF TREFOIL MOTIF CONTAINING CELL-GROWTH FACTORS

被引:55
作者
CARR, MD
机构
[1] Laboratory of Molecular Structure, National Institute for Medical Research, London, The Ridgeway, Mill Hill
关键词
D O I
10.1021/bi00122a015
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
Two-dimensional H-1 NMR spectroscopy has been used to obtain comprehensive sequence-specific resonance assignments for the putative cell growth factor porcine pancreatic spasmolytic polypeptide, which is a 106-residue protein containing two "trefoil" domains. The patterns of sequential (i,i + 1), medium-range (i,i < 5), and long-range NH to NH, alpha-CH to NH, and alpha-CH to alpha-CH nuclear Overhauser effects clearly show that the protein's two trefoil domains adopt essentially the same secondary structure in solution. The main feature of each domain is a seven-residue helix followed by a short antiparallel beta-sheet formed from two strands of four amino acids each. This is a novel supersecondary structure, which clearly identifies the trefoil motif as a new class of growth factor associated module, distinct from other types of highly disulfide cross-linked domains, such as those found in epidermal growth factor and insulin-like growth factor I.
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页码:1998 / 2004
页数:7
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