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A second crystal structure of human mucosal addressin cell-adhesion molecule reveals that strand swapping can lead to dimer assembly and alters the conformation of the proposed integrin-binding surface.

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The crystal structure of a mouse phosphatidylethanolamine-binding protein homologue (mPEBP-2) has been determined to 1.8 Å. Regions of distinctive sequence associated with the PEBP-2 subset identified from alignments of the PEBP family are discussed with reference to the structure.
Keywords: PEBPs.
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