2KCF

The NMR solution structure of the isolated Apo Pin1 WW domain

Summary for 2KCF

• Entry DOI: 10.2210/pdb2kcf/pdb
• Related: 2kbu
• Descriptor: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (1 entity in total)
• Functional Keywords: isomerase, peptidylprolyl isomerase, pin1, ww domain, cell cycle, nucleus, phosphoprotein, rotamase
• Biological source: Homo sapiens
• Cellular location: Nucleus: Q13526
• Total number of polymer chains: 1
• Total formula weight: 4174.64

Authors

Kowalski, J.A.,Liu, K.,Kelly, J.W. (deposition date: 2008-12-19, release date: 2009-01-13, Last modification date: 2024-05-22)

Primary citation

Kowalski, J.A.,Liu, K.,Kelly, J.W.
NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1
Biopolymers, 63:111-121, 2002

PubMed Abstract: The NMR solution structure of the isolated Apo Pin1 WW domain (6-39) reveals that it adopts a twisted three-stranded antiparallel beta-sheet conformation, very similar to the structure exhibited by the crystal of this domain in the context of the two domain Pin1 protein. While the B factors in the apo x-ray crystal structure indicate that loop 1 and loop 2 are conformationally well defined, the solution NMR data suggest that loop 1 is quite flexible, at least in the absence of the ligand. The NMR chemical shift and nuclear Overhauser effect pattern exhibited by the 6-39 Pin1 WW domain has proven to be diagnostic for demonstrating that single site variants of this domain adopt a normally folded structure. Knowledge of this type is critical before embarking on time-consuming kinetic and thermodynamic studies required for a detailed understanding of beta-sheet folding.

PubMed: 11786999

Experimental method

SOLUTION NMR