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| | {{STRUCTURE_1smb| PDB=1smb | SCENE= }} | | {{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=== |
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| - | ==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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15123429}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15123429 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15123429}} |
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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]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:52:48 2008'' | + | |
| | + | ''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
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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