Molecular characterization of the Ran-binding zinc finger domain of Nup153.

Molecular characterization of the Ran-binding zinc finger domain of Nup153. Research Abstract Details 

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Molecular characterization of the Ran-binding zinc finger domain of Nup153. Abstract Text:

Meda M Higa,Steven L Alam,Wesley I Sundquist,Katharine S Ullman,

The nuclear pore complex is the gateway for selective traffic between the nucleus and cytoplasm. To learn how building blocks of the pore can create specific docking sites for transport receptors and regulatory factors, we have studied a zinc finger module present in multiple copies within the nuclear pores of higher eukaryotes. All four zinc fingers of human Nup153 were found to bind the small GTPase Ran with dissociation constants ranging between 5 and 40 mum. In addition a fragment of Nup153 encompassing the four tandem zinc fingers was found to bind Ran with similar affinity. NMR structural studies revealed that a representative Nup153 zinc finger adopts the same zinc ribbon structure as the previously characterized Npl4 NZF module. Ran binding was mediated by a three-amino acid motif (Leu(13)/Val(14)/Asn(25)) located within the two zinc coordination loops. Nup153 ZnFs bound GDP and GTP forms of Ran with similar affinities, indicating that this interaction is not influenced by a nucleotide-dependent conformational switch. Taken together, these studies elucidate the Ran-binding interface on Nup153 and, more broadly, provide insight into the versatility of this zinc finger binding module.

Molecular characterization of the Ran-binding zinc finger domain of Nup153. Publishing Authors By Initials

MM Higa,SL Alam,WI Sundquist,KS Ullman,

For similar enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: ran gtp-binding protein research abstracts see: enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: ran gtp-binding protein research

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Molecular characterization of the Ran-binding zinc finger domain of Nup153. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 17090-100

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 10

MONTH: 04

YEAR: 2007

Molecular characterization of the Ran-binding zinc finger domain of Nup153. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Molecular characterization of the Ran-binding zinc finger domain of Nup153. Keywords Mesh Terms:

KEYWORDS: ran GTP-Binding Protein

MESH TERMS: metabolism

Chemical & Substance for Abstract: Molecular characterization of the Ran-binding zinc finger domain of Nup153. Information

Substance Name: ran GTP-Binding Protein

Registry Number: EC 3.6.5.2

Grant and Affiliation Information for Molecular characterization of the Ran-binding zinc finger domain of Nup153.

AFFILIATION: Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah, Salt Lake City, Utah 84112, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: T32 GM07464

ACRONYM: GM

MEDLINETA: J Biol Chem

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