Does structure of a PH domain from the C. elegans muscle protein UNC-89 suggest a novel function?
We present the first structure of a PH domain with a strong negative overall electrostatic potential. The presence of a deep pocket lined with negative charges suggests that the domain binds to ligands other than acidic phospholipids. The abundance of this class of PH domain in the C. elegans genome suggests a prominent role in mediating protein-protein interactions.
On-site diagnostic service availability may contribute to unnecessary biopsies, but does not explain the higher diagnostic mammography false-positive rates at facilities serving vulnerable women.