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1pxu

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(New page: 200px<br /><applet load="1pxu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pxu, resolution 2.20&Aring;" /> '''Crystal structure of...)
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[[Image:1pxu.gif|left|200px]]<br /><applet load="1pxu" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pxu.gif|left|200px]]<br /><applet load="1pxu" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pxu, resolution 2.20&Aring;" />
caption="1pxu, resolution 2.20&Aring;" />
'''Crystal structure of chicken NtA from a eukaryotic source at 2.2A resolution'''<br />
'''Crystal structure of chicken NtA from a eukaryotic source at 2.2A resolution'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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1PXU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA].
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1PXU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXU OCA].
==Reference==
==Reference==
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[[Category: agrin]]
[[Category: agrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:13:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:41 2008''

Revision as of 12:33, 21 February 2008


1pxu, resolution 2.20Å

Drag the structure with the mouse to rotate

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

Overview

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.

About this Structure

1PXU is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Structure and laminin-binding specificity of the NtA domain expressed in eukaryotic cells., Mascarenhas JB, Ruegg MA, Sasaki T, Eble JA, Engel J, Stetefeld J, Matrix Biol. 2005 Jan;23(8):507-13. Epub 2004 Dec 30. PMID:15694127

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