1FHO

Solution Structure of the PH Domain from the C. Elegans Muscle Protein UNC-89

Summary for 1FHO

• Entry DOI: 10.2210/pdb1fho/pdb
• NMR Information: BMRB: 4373
• Descriptor: UNC-89 (1 entity in total)
• Functional Keywords: pleckstrin homology domain, electrostatics, muscle, signal transduction, signaling protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 1
• Total formula weight: 14103.74

Authors

Blomberg, N.,Baraldi, E.,Sattler, M.,Saraste, M.,Nilges, M. (deposition date: 2000-08-02, release date: 2000-10-04, Last modification date: 2024-05-22)

Primary citation

Blomberg, N.,Baraldi, E.,Sattler, M.,Saraste, M.,Nilges, M.
Structure of a PH domain from the C. elegans muscle protein UNC-89 suggests a novel function.
Structure Fold.Des., 8:1079-1087, 2000

PubMed Abstract: Pleckstrin homology (PH) domains constitute a structurally conserved family present in many signaling and regulatory proteins. PH domains have been shown to bind to phospholipids, and many function in membrane targeting. They generally have a strong electrostatic polarization and interact with negatively charged phospholipids via the positive pole. On the basis of electrostatic modeling, however, we have previously identified a class of PH domains with a predominantly negative charge and predicted that these domains recognize other targets. Here, we report the first experimental structure of such a PH domain.

PubMed: 11080629
DOI: 10.1016/S0969-2126(00)00509-8

Experimental method

SOLUTION NMR