Document Detail

Nuclear magnetic resonance solution and X-ray structures of squash trypsin inhibitor exhibit the same conformation of the proteinase binding loop.
MedLine Citation:
PMID:  2614838     Owner:  NLM     Status:  MEDLINE    
A comparison of the solution nuclear magnetic resonance (n.m.r.) structures of squash trypsin inhibitor from seeds of the squash Cucurbita maxima with the X-ray structure of a trypsin complex of the inhibitor shows that the n.m.r. and X-ray structures are similar in terms of the global folding and secondary structure. The average atomic root-mean-square difference between the 36 n.m.r. structures on the one hand and the X-ray structure is 0.96 A for the backbone atoms and 1.95 A for all heavy atoms. The n.m.r. and X-ray structures exhibit extremely similar conformations of the primary proteinase binding loop. Despite the overall similarity, there are small differences between the mean computed structure and the X-ray structure. The n.m.r. structures have slightly different positions of the segments from residues 16 to 18, and 24 and 25. The n.m.r. results show that the inclusion of stereospecific assignments and precise distance constraints results in a significant improvement in the definition of the n.m.r. structure, making possible a detailed analysis of the local conformations in the protein.
T A Holak; W Bode; R Huber; J Otlewski; T Wilusz
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of molecular biology     Volume:  210     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  1989 Dec 
Date Detail:
Created Date:  1990-02-23     Completed Date:  1990-02-23     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  649-54     Citation Subset:  IM    
Max-Planck-Institut für Biochemie, Martinsried bei München, FRG.
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MeSH Terms
Binding Sites
Hydrogen Bonding
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Plant Proteins / ultrastructure*
Trypsin Inhibitors / ultrastructure*
X-Ray Diffraction
Reg. No./Substance:
0/Plant Proteins; 0/Solutions; 0/Trypsin Inhibitors

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