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{{STRUCTURE_1smb|  PDB=1smb  |  SCENE=  }}  
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'''Crystal Structure of Golgi-Associated PR-1 protein'''
===Crystal Structure of Golgi-Associated PR-1 protein===




==Overview==
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The plant pathogenesis related proteins group 1 (PR-1) and a variety of related mammalian proteins constitute a PR-1 protein family that share sequence and structural similarities. GAPR-1 is a unique family member as thus far it is the only PR-1 family member that is not co-translationally targeted to the lumen of the endoplasmic reticulum before trafficking to either vacuoles or secretion. Here we report that GAPR-1 may form dimers in vitro and in vivo, as determined by yeast two-hybrid screening, biochemical and biophysical assays. The 1.55A crystal structure demonstrates that GAPR-1 is structurally homologous to the other PR-1 family members previously solved (p14a and Ves V 5). Through an examination of inter-molecular interactions between GAPR-1 molecules in the crystal lattice, we propose a number of the highly conserved amino acid residues of the PR-1 family to be involved in the regulation of dimer formation of GAPR-1 with potential implications for other PR-1 family members. We show that mutagenesis of these conserved amino acid residues leads to a greatly increased dimer population. A recent report suggests that PR-1 family members may exhibit serine protease activity and further examination of the dimer interface of GAPR-1 indicates that a catalytic triad similar to that of serine proteases may be formed across the dimer interface by residues from both molecules within the dimer.
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==About this Structure==
==About this Structure==
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[[Category: Sinning, I.]]
[[Category: Sinning, I.]]
[[Category: Alpha-beta-alpha]]
[[Category: Alpha-beta-alpha]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:29:11 2008''

Revision as of 14:29, 28 July 2008

File:1smb.png

Template:STRUCTURE 1smb

Crystal Structure of Golgi-Associated PR-1 protein

Template:ABSTRACT PUBMED 15123429

About this Structure

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

Reference

Structural analysis of the human Golgi-associated plant pathogenesis related protein GAPR-1 implicates dimerization as a regulatory mechanism., Serrano RL, Kuhn A, Hendricks A, Helms JB, Sinning I, Groves MR, J Mol Biol. 2004 May 21;339(1):173-83. PMID:15123429

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