1yg9: Difference between revisions

Revision as of 17:05, 21 February 2008

The structure of mutant (N93Q) of bla g 2

OverviewOverview

The crystal structure of Bla g 2 was solved in order to investigate the structural basis for the allergenic properties of this unusual protein. This is the first structure of an aspartic protease in which conserved glycine residues, in two canonical DTG triads, are substituted by different amino acid residues. Another unprecedented feature revealed by the structure is the single phenylalanine residue insertion on the tip of the flap, with the side-chain occupying the S1 binding pocket. This and other important amino acid substitutions in the active site region of Bla g 2 modify the interactions in the vicinity of the catalytic aspartate residues, increasing the distance between them to approximately 4A and establishing unique direct contacts between the flap and the catalytic residues. We attribute the absence of substantial catalytic activity in Bla g 2 to these unusual features of the active site. Five disulfide bridges and a Zn-binding site confer stability to the protein, which may contribute to sensitization at lower levels of exposure than other allergens.

About this StructureAbout this Structure

1YG9 is a Single protein structure of sequence from Blattella germanica with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition., Gustchina A, Li M, Wunschmann S, Chapman MD, Pomes A, Wlodawer A, J Mol Biol. 2005 Apr 29;348(2):433-44. PMID:15811379

Page seeded by OCA on Thu Feb 21 16:05:02 2008

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OCA

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-[[Image:1yg9.gif|left|200px]]<br /><applet load="1yg9" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1yg9.gif|left|200px]]<br /><applet load="1yg9" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1yg9, resolution 1.30&Aring;" />
 '''The structure of mutant (N93Q) of bla g 2'''<br />
 ==Overview==
-The crystal structure of Bla g 2 was solved in order to investigate the, structural basis for the allergenic properties of this unusual protein., This is the first structure of an aspartic protease in which conserved, glycine residues, in two canonical DTG triads, are substituted by, different amino acid residues. Another unprecedented feature revealed by, the structure is the single phenylalanine residue insertion on the tip of, the flap, with the side-chain occupying the S1 binding pocket. This and, other important amino acid substitutions in the active site region of Bla, g 2 modify the interactions in the vicinity of the catalytic aspartate, residues, increasing the distance between them to approximately 4A and, establishing unique direct contacts between the flap and the catalytic, residues. We attribute the absence of substantial catalytic activity in, Bla g 2 to these unusual features of the active site. Five disulfide, bridges and a Zn-binding site confer stability to the protein, which may, contribute to sensitization at lower levels of exposure than other, allergens.
+The crystal structure of Bla g 2 was solved in order to investigate the structural basis for the allergenic properties of this unusual protein. This is the first structure of an aspartic protease in which conserved glycine residues, in two canonical DTG triads, are substituted by different amino acid residues. Another unprecedented feature revealed by the structure is the single phenylalanine residue insertion on the tip of the flap, with the side-chain occupying the S1 binding pocket. This and other important amino acid substitutions in the active site region of Bla g 2 modify the interactions in the vicinity of the catalytic aspartate residues, increasing the distance between them to approximately 4A and establishing unique direct contacts between the flap and the catalytic residues. We attribute the absence of substantial catalytic activity in Bla g 2 to these unusual features of the active site. Five disulfide bridges and a Zn-binding site confer stability to the protein, which may contribute to sensitization at lower levels of exposure than other allergens.
 ==About this Structure==
-YG9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Blattella_germanica Blattella germanica] with NAG and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YG9 OCA].
+YG9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Blattella_germanica Blattella germanica] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YG9 OCA].
 ==Reference==
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 [[Category: bla g 2]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:45:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:02 2008''