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| - | [[Image:1xf5.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1xf5.png|left|200px]] |
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| | {{STRUCTURE_1xf5| PDB=1xf5 | SCENE= }} | | {{STRUCTURE_1xf5| PDB=1xf5 | SCENE= }} |
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| - | '''Complex HCV core-Fab 19D9D6-Protein L mutant (H74C, Y64W)in space group P21212'''
| + | ===Complex HCV core-Fab 19D9D6-Protein L mutant (H74C, Y64W)in space group P21212=== |
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| - | ==Overview==
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| - | Proteins and peptides with variable degrees of disorder are a challenge for protein crystallization. These may be completely disordered or just contain regions with a high degree of mobility that may be represented by a multitude of discretely defined conformations. These difficulties are not insurmountable, but it may be unreasonable to expect a clean result from a structural point of view. The complex between a murine monoclonal antibody (19D9D6) and a synthetic peptide that encompasses the first 45 residues of the core protein of Hepatitis C virus that is poorly structured in solution has been crystallized. In order to make the crystallization possible, use was made of a single immunoglobulin-binding domain of protein L from Peptostreptococcus magnus (PpL), a bacterial protein that can bind the variable region (Fv) of a large population of antibodies through its light chain with no interference with antibody-antigen recognition. Crystals were obtained in different space groups where the size of the cavity that accommodates the peptide is different, although many of the crystal contacts and the overall lattice are preserved. The peptide can be considered to be semi-disordered and the larger cavity accommodates a better ordered peptide than the smaller one. The lattice is of interest for the design of a scaffold system for the crystallization of peptide-tagged proteins since a cavity that accommodates a disordered entity might be able to host ordered proteins of the same size and shape as the cavity. Here, the differences between the lattices formed by this trimolecular complex are described and it is discussed how such a system may be adapted to the crystallization of peptide-tagged proteins.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15930632}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15930632 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15930632}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Peptide complex]] | | [[Category: Peptide complex]] |
| | [[Category: Protein l]] | | [[Category: Protein l]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:56:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:38:25 2008'' |
Revision as of 13:38, 29 July 2008
Template:STRUCTURE 1xf5
Complex HCV core-Fab 19D9D6-Protein L mutant (H74C, Y64W)in space group P21212
Template:ABSTRACT PUBMED 15930632
About this Structure
1XF5 is a Single protein structure of sequence from Finegoldia magna and Mus musculus. Full crystallographic information is available from OCA.
Reference
Different crystal packing in Fab-protein L semi-disordered peptide complex., Menez R, Housden NG, Harrison S, Jolivet-Reynaud C, Gore MG, Stura EA, Acta Crystallogr D Biol Crystallogr. 2005 Jun;61(Pt 6):744-9. Epub 2005, May 26. PMID:15930632
Page seeded by OCA on Tue Jul 29 16:38:25 2008
