1UP1

UP1, THE TWO RNA-RECOGNITION MOTIF DOMAIN OF HNRNP A1

Summary for 1UP1

• Entry DOI: 10.2210/pdb1up1/pdb
• Descriptor: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (2 entities in total)
• Functional Keywords: nuclear proteinhnrnp a1, rna-recognition motif, rna-binding, up1, nuclear protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P09651
• Total number of polymer chains: 1
• Total formula weight: 20834.46

Authors

Xu, R.-M.,Jokhan, L.,Cheng, X.,Mayeda, A.,Krainer, A.R. (deposition date: 1997-03-12, release date: 1997-09-17, Last modification date: 2024-02-14)

Primary citation

Xu, R.M.,Jokhan, L.,Cheng, X.,Mayeda, A.,Krainer, A.R.
Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs.
Structure, 5:559-570, 1997

PubMed Abstract: Heterogeneous nuclear ribonucleoprotein (hnRNP) A1 is one of the most abundant core proteins of hnRNP complexes in metazoan nuclei. It behaves as a global regulator of alternative pre-mRNA splicing by antagonizing the activities of several serine/arginine-rich splicing factors (SR proteins), resulting in the activation of distal alternative 5' splice sites and skipping of optional exons. Purified hnRNP A1 has nucleic acid annealing activity. The protein also shuttles continuously between the nucleus and the cytoplasm, a process mediated by signals within its C-terminal glycine-rich domain. The N-terminal region of human hnRNP A1, termed unwinding protein 1 (UP1), contains two RNA-recognition motifs (RRMs), RRM1 and RRM2. Understanding the structural elements by which hnRNP A1 interacts with RNA will have broad implications for studies of RNA processing.

PubMed: 9115444
DOI: 10.1016/S0969-2126(97)00211-6

Experimental method

X-RAY DIFFRACTION (1.9 Å)