2jnb

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|ACTIVITY=
|ACTIVITY=
|GENE= NHP2L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= NHP2L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jnb OCA], [http://www.ebi.ac.uk/pdbsum/2jnb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jnb RCSB]</span>
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[[Category: splicing]]
[[Category: splicing]]
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Revision as of 00:59, 31 March 2008


PDB ID 2jnb

Drag the structure with the mouse to rotate
Gene: NHP2L1 (Homo sapiens)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Solution Structure of RNA-binding protein 15.5K


Overview

The kink-turn (K-turn) motif is recognized and bound by a family of proteins that act as nucleation factors for ribonucleoparticle assembly. The binding of various proteins to a conserved RNA structural motif known as the K-turn has been shown to be an important component of regulation in the ribosome, in the spliceosome, and in RNA modification. 15.5K is a prototypical example of a K-turn binding protein, which has been shown to bind the 5'-U4 stem-loop of the spliceosome and the box C/D motif. We describe the solution NMR structure of free 15.5K, as well as studies of conformational flexibility from 15N NMR relaxation and H/D exchange experiments. The protein appears well-structured aside from conformational fluctuation in alpha3. Flexibility in fast time scale motions and the observation of limited intermediate and slow motions further characterize the free protein and may suggest local contributions to recognition and binding.

About this Structure

2JNB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Functional implications for a prototypical K-turn binding protein from structural and dynamical studies of 15.5K., Soss SE, Flynn PF, Biochemistry. 2007 Dec 25;46(51):14979-86. Epub 2007 Nov 29. PMID:18044964

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