1IB2

CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN

Summary for 1IB2

• Entry DOI: 10.2210/pdb1ib2/pdb
• Related: 1IB3
• Descriptor: PUMILIO 1, BETA-MERCAPTOETHANOL (3 entities in total)
• Functional Keywords: pumilio-homology domain, puf motif, rna binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 40442.66

Authors

Wang, X.,Zamore, P.D.,Hall, T.M.T. (deposition date: 2001-03-26, release date: 2001-05-09, Last modification date: 2025-03-26)

Primary citation

Wang, X.,Zamore, P.D.,Hall, T.M.
Crystal structure of a Pumilio homology domain.
Mol.Cell, 7:855-865, 2001

PubMed Abstract: Puf proteins regulate translation and mRNA stability by binding sequences in their target RNAs through the Pumilio homology domain (PUM-HD), which is characterized by eight tandem copies of a 36 amino acid motif, the PUM repeat. We have solved the structure of the PUM-HD from human Pumilio1 at 1.9 A resolution. The structure reveals that the eight PUM repeats correspond to eight copies of a single, repeated structural motif. The PUM repeats pack together to form a right-handed superhelix that approximates a half doughnut. The distribution of side chains on the inner and outer faces of this half doughnut suggests that the inner face of the PUM-HD binds RNA while the outer face interacts with proteins such as Nanos, Brain Tumor, and cytoplasmic polyadenylation element binding protein.

PubMed: 11336708
DOI: 10.1016/S1097-2765(01)00229-5

Experimental method

X-RAY DIFFRACTION (1.9 Å)