1xct: Difference between revisions

Revision as of 16:53, 21 February 2008

Complex HCV core-Fab 19D9D6-Protein L mutant (D55A, L57H, Y64W) in space group P21212

OverviewOverview

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.

About this StructureAbout this Structure

1XCT is a Single protein structure of sequence from Finegoldia magna and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 15:53:25 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1xct.gif|left|200px]]<br />
+[[Image:1xct.gif|left|200px]]<br /><applet load="1xct" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1xct" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1xct, resolution 3.05&Aring;" />
 '''Complex HCV core-Fab 19D9D6-Protein L mutant (D55A, L57H, Y64W) in space group P21212'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-XCT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XCT OCA].
+XCT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XCT OCA].
 ==Reference==
@@ Line 15: / Line 14: @@
 [[Category: Mus musculus]]
 [[Category: Single protein]]
-[[Category: Gore, M.G.]]
+[[Category: Gore, M G.]]
 [[Category: Harrison, S.]]
-[[Category: Housden, N.G.]]
+[[Category: Housden, N G.]]
 [[Category: Jolivet-Reynaud, C.]]
 [[Category: Menez, R.]]
-[[Category: Stura, E.A.]]
+[[Category: Stura, E A.]]
 [[Category: crystal packing]]
 [[Category: fab]]
@@ Line 26: / Line 25: @@
 [[Category: protein l]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:44:20 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:53:25 2008''