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Residues 82 to 106 of BPI show limited sequence similarity with residues 32 to 51 of the limulus anti-LPS factor (LALF) and have been predicted to form an amphipathic β hairpin similar to that seen in the LALF structure (21). Although this region of BPI does form a β hairpin, the strict amphipathic character of the loop seen in LALF is not maintained, and a structural superposition shows that the sequence of BPI must be shifted by one residue relative to the proposed sequence alignment.
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note
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We thank S. Abrahamson, E. Bautista, P. Gavit, A. Horwitz, G. Theofan, and J. Weickmann for protein preparation, T. Le for crystallization, R. Liddington for coordinates of LALF, M. Stowell for use of the xenon pressure apparatus, K. Faull for mass spectrometry, and M. Bennett and M. Weiss for discussions. Supported by NIH grant GM31299 and by the U.S. Department of Energy. Coordinates have been deposited in the Brookhaven Protein Data Bank (ID code 1bp1).
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