1PLS

SOLUTION STRUCTURE OF A PLECKSTRIN HOMOLOGY DOMAIN

Summary for 1PLS

• Entry DOI: 10.2210/pdb1pls/pdb
• Descriptor: PLECKSTRIN HOMOLOGY DOMAIN (1 entity in total)
• Functional Keywords: phosphorylation
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 13341.48

Authors

Yoon, H.S.,Hajduk, P.J.,Petros, A.M.,Olejniczak, E.T.,Meadows, R.P.,Fesik, S.W. (deposition date: 1994-05-03, release date: 1995-06-03, Last modification date: 2024-05-01)

Primary citation

Yoon, H.S.,Hajduk, P.J.,Petros, A.M.,Olejniczak, E.T.,Meadows, R.P.,Fesik, S.W.
Solution structure of a pleckstrin-homology domain.
Nature, 369:672-675, 1994

PubMed Abstract: Pleckstrin, the major protein kinase C substrate of platelets, contains domains of about 100 amino acids at the amino and carboxy termini that have been found in a number of proteins, including serine/threonine kinases, GTPase-activating proteins, phospholipases and cytoskeletal proteins. These conserved sequences, termed pleckstrin-homology (PH) domains, are thought to be involved in signal transduction. But the details of the function and binding partners of the PH domains have not been characterized. Here we report the solution structure of the N-terminal pleckstrin-homology domain of pleckstrin determined using heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. The structure consists of an up-and-down beta-barrel of seven antiparallel beta-strands and a C-terminal amphiphilic alpha-helix that caps one end of the barrel. The overall topology of the domain is similar to that of the retinol-binding protein family of structures.

PubMed: 8208296
DOI: 10.1038/369672a0

Experimental method

SOLUTION NMR