1snl

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spinqualitylabelsall models PDB ID 1snl Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
Gene:	NUCB1, NUC (Homo sapiens)
Related:	1CMF, 1CMG, 1CLL, 1A2X, 1BLQ
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

NMR Solution Structure of the Calcium-binding Domain of Nucleobindin (CALNUC)

Overview

Nucleobindin, also known as calnuc, participates in Ca2+ storage in the Golgi, as well as in other biological processes that involve DNA-binding and protein-protein interactions. We have determined the three-dimensional solution structure of the Ca(2+)-binding domain of nucleobindin by NMR showing that it consists of two EF-hand motifs. The NMR structure indicates that the phi and psi angles of residues in both motifs are very similar, despite the noncanonical sequence of the C-terminal EF-hand, which contains an arginine residue instead of the typical glycine at the sixth position of the 12-residue loop. The relative orientation of the alpha-helices in the N-terminal EF-hand falls within the common arrangement found in most EF-hand structures. In contrast, the noncanonical EF-hand deviates from the average orientation. The two helix-loop-helix moieties are in the open conformation characteristic of the Ca(2+)-bound state. We find that both motifs bind Ca2+ with apparent dissociation constants of 47 and 40 microM for the noncanonical and the canonical EF-hand, respectively. The Ca(2+)-binding domain of nucleobindin is unstructured in the absence of Ca2+ and folds upon Ca2+ addition. NMR relaxation data and structural studies of the folded domain indicate that it undergoes slow dynamics, suggesting that it is floppier and less compact than a globular domain.

About this Structure

1SNL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural studies on the Ca2+-binding domain of human nucleobindin (calnuc)., de Alba E, Tjandra N, Biochemistry. 2004 Aug 10;43(31):10039-49. PMID:15287731

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