1DFJ

RIBONUCLEASE INHIBITOR COMPLEXED WITH RIBONUCLEASE A

Summary for 1DFJ

• Entry DOI: 10.2210/pdb1dfj/pdb
• Descriptor: RIBONUCLEASE A, RIBONUCLEASE INHIBITOR, SULFATE ION, ... (4 entities in total)
• Functional Keywords: complex (ribonuclease-inhibitor), ribonuclease, hydrolase, leucine-rich repeats, complex (endonuclease-inhibitor) complex, complex (endonuclease/inhibitor)
• Biological source: Bos taurus (cattle); More
• Cellular location: Secreted: P61823; Cytoplasm: P10775
• Total number of polymer chains: 2
• Total formula weight: 62896.55

Authors

Kobe, B.,Deisenhofer, J. (deposition date: 1996-06-29, release date: 1997-01-11, Last modification date: 2024-10-16)

Primary citation

Kobe, B.,Deisenhofer, J.
A structural basis of the interactions between leucine-rich repeats and protein ligands.
Nature, 374:183-186, 1995

PubMed Abstract: The leucine-rich repeat is a recently characterized structural motif used in molecular recognition processes as diverse as signal transduction, cell adhesion, cell development, DNA repair and RNA processing. We present here the crystal structure at 2.5 A resolution of the complex between ribonuclease A and ribonuclease inhibitor, a protein built entirely of leucine-rich repeats. The unusual non-globular structure of ribonuclease inhibitor, its solvent-exposed parallel beta-sheet and the conformational flexibility of the structure are used in the interaction; they appear to be the principal reasons for the effectiveness of leucine-rich repeats as protein-binding motifs. The structure can serve as a model for the interactions of other proteins containing leucine-rich repeats with their ligands.

PubMed: 7877692
DOI: 10.1038/374183a0

Experimental method

X-RAY DIFFRACTION (2.5 Å)