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PDBsum entry 1pz8

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Structural protein PDB id
1pz8
Contents
Protein chains
176 a.a. *
Metals
_CA ×4
Waters ×569
* Residue conservation analysis

References listed in PDB file
Key reference
Title Modulation of agrin function by alternative splicing and ca2+ binding.
Authors J.Stetefeld, A.T.Alexandrescu, M.W.Maciejewski, M.Jenny, K.Rathgeb-Szabo, T.Schulthess, R.Landwehr, S.Frank, M.A.Ruegg, R.A.Kammerer.
Ref. Structure, 2004, 12, 503-515. [DOI no: 10.1016/j.str.2004.02.001]
PubMed id 15016366
Abstract
The aggregation of acetylcholine receptors on postsynaptic membranes is a key step in neuromuscular junction development. This process depends on alternatively spliced forms of the proteoglycan agrin with "B-inserts" of 8, 11, or 19 residues in the protein's globular C-terminal domain, G3. Structures of the neural B8 and B11 forms of agrin-G3 were determined by X-ray crystallography. The structure of G3-B0, which lacks inserts, was determined by NMR. The agrin-G3 domain adopts a beta jellyroll fold. The B insert site is flanked by four loops on one edge of the beta sandwich. The loops form a surface that corresponds to a versatile interaction interface in the family of structurally related LNS proteins. NMR and X-ray data indicate that this interaction interface is flexible in agrin-G3 and that flexibility is reduced by Ca(2+) binding. The plasticity of the interaction interface could enable different splice forms of agrin to select between multiple binding partners.
Figure 7.
Figure 7. Comparison of Charge Distribution in Calcium Bound G Domains(A) The G5 domain of the a2 chain of laminin (Hohenester et al., 1999). Basic residues important in binding of a-DG to laminin are labeled green.(B) Calcium-bound NMR structure of the agrin-G3 B0 domain.(C) Calcium-bound B8 X-ray structure.(D) Calcium-bound B11 X-ray structure. The calcium binding site is indicated in the laminin structure, but is left out for clarity in the agrin structures (conserved red cavity). The GRASP diagrams were made using the "full.crg" charge/radius file and are colored according to an electrostatic potential ramp ranging from +5 e kT -1 (blue, positive) to -5 e kT -1 (red, negative). The calcium ion was not included in electrostatic calculations. The position of the calcium binding site (conserved red cavity) is indicated in the laminin structure.
The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 503-515) copyright 2004.
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