1pxu: Difference between revisions

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[[Image:1pxu.gif|left|200px]]
{{Seed}}
[[Image:1pxu.png|left|200px]]


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{{STRUCTURE_1pxu|  PDB=1pxu  |  SCENE=  }}  
{{STRUCTURE_1pxu|  PDB=1pxu  |  SCENE=  }}  


'''Crystal structure of chicken NtA from a eukaryotic source at 2.2A resolution'''
===Crystal structure of chicken NtA from a eukaryotic source at 2.2A resolution===




==Overview==
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Agrin is a key organizer for postsynaptic differentiation at the neuromuscular junction (NMJ). This activity requires the binding of agrin to the synaptic basal lamina via its N-terminal (NtA) domain. It has been suggested that this binding is mediated by conserved amino acids in the gamma 1 chain of laminin. Here, we report the crystal structure of chicken NtA expressed in eukaryotic HEK293 cells. In contrast to the previously published structure [Stetefeld, J., Jenny, M., Schulthess, T., Landwehr, R., Schumacher, B., Frank, S., Ruegg, M.A., Engel, J., Kammerer, R.A., 2001. The laminin-binding domain of agrin is structurally related to N-TIMP-1. Nat. Struct. Biol., 8, 705-709.], which was derived from the NtA domain expressed in E. coli, the new data show that the N-terminal tail region (amino acid residues Asn1-Arg5) is highly structured. Moreover, the disulfide bridge between Cys2 and Cys74 was also present. In addition, we show that the binding of NtA requires the gamma 1 chain of laminin and is not greatly affected by the composition of beta chains. These results confirm a model of the NtA-laminin complex where conserved amino acids in the gamma 1 chain are prerequisite for the binding to agrin and they further emphasize that the source of protein can be critical in structure determination.
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{{ABSTRACT_PUBMED_15694127}}


==About this Structure==
==About this Structure==
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[[Category: Stetefeld, J.]]
[[Category: Stetefeld, J.]]
[[Category: Agrin]]
[[Category: Agrin]]
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