1ztp: Difference between revisions

Revision as of 17:19, 21 February 2008

X-ray structure of gene product from homo sapiens Hs.433573

OverviewOverview

The crystal structure of the human basophilic leukemia-expressed protein (BLES03, p5326, Hs.433573) was determined by single-wavelength anomalous diffraction and refined to an R factor of 18.8% (Rfree = 24.5%) at 2.5 A resolution. BLES03 shows no detectable sequence similarity to any functionally characterized proteins using state-of-the-art sequence-comparison tools. The structure of BLES03 adopts a fold similar to that of eukaryotic transcription initiation factor 4E (eIF4E), a protein involved in the recognition of the cap structure of eukaryotic mRNA. In addition to fold similarity, the electrostatic surface potentials of BLES03 and eIF4E show a clear conservation of basic and acidic patches. In the crystal lattice, the acidic amino-terminal helices of BLES03 monomers are bound within the basic cavity of symmetry-related monomers in a manner analogous to the binding of mRNA by eIF4E. Interestingly, the gene locus encoding BLES03 is located between genes encoding the proteins DRAP1 and FOSL1, both of which are involved in transcription initiation. It is hypothesized that BLES03 itself may be involved in a biochemical process that requires recognition of nucleic acids.

About this StructureAbout this Structure

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

ReferenceReference

The structure at 2.5 A resolution of human basophilic leukemia-expressed protein BLES03., Bitto E, Bingman CA, Robinson H, Allard ST, Wesenberg GE, Phillips GN Jr, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Sep 1;61(Pt, 9):812-7. Epub 2005 Aug 31. PMID:16511166

Page seeded by OCA on Thu Feb 21 16:18:58 2008

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OCA

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 ==Overview==
-The crystal structure of the human basophilic leukemia-expressed protein, (BLES03, p5326, Hs.433573) was determined by single-wavelength anomalous, diffraction and refined to an R factor of 18.8% (Rfree = 24.5%) at 2.5 A, resolution. BLES03 shows no detectable sequence similarity to any, functionally characterized proteins using state-of-the-art, sequence-comparison tools. The structure of BLES03 adopts a fold similar, to that of eukaryotic transcription initiation factor 4E (eIF4E), a, protein involved in the recognition of the cap structure of eukaryotic, mRNA. In addition to fold similarity, the electrostatic surface potentials, of BLES03 and eIF4E show a clear conservation of basic and acidic patches., In the crystal lattice, the acidic amino-terminal helices of BLES03, monomers are bound within the basic cavity of symmetry-related monomers in, a manner analogous to the binding of mRNA by eIF4E. Interestingly, the, gene locus encoding BLES03 is located between genes encoding the proteins, DRAP1 and FOSL1, both of which are involved in transcription initiation., It is hypothesized that BLES03 itself may be involved in a biochemical, process that requires recognition of nucleic acids.
+The crystal structure of the human basophilic leukemia-expressed protein (BLES03, p5326, Hs.433573) was determined by single-wavelength anomalous diffraction and refined to an R factor of 18.8% (Rfree = 24.5%) at 2.5 A resolution. BLES03 shows no detectable sequence similarity to any functionally characterized proteins using state-of-the-art sequence-comparison tools. The structure of BLES03 adopts a fold similar to that of eukaryotic transcription initiation factor 4E (eIF4E), a protein involved in the recognition of the cap structure of eukaryotic mRNA. In addition to fold similarity, the electrostatic surface potentials of BLES03 and eIF4E show a clear conservation of basic and acidic patches. In the crystal lattice, the acidic amino-terminal helices of BLES03 monomers are bound within the basic cavity of symmetry-related monomers in a manner analogous to the binding of mRNA by eIF4E. Interestingly, the gene locus encoding BLES03 is located between genes encoding the proteins DRAP1 and FOSL1, both of which are involved in transcription initiation. It is hypothesized that BLES03 itself may be involved in a biochemical process that requires recognition of nucleic acids.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-The structure at 2.5 A resolution of human basophilic leukemia-expressed protein BLES03., Bitto E, Bingman CA, Robinson H, Allard ST, Wesenberg GE, Phillips GN Jr, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Sep 1;61(Pt, 9):812-7. Epub 2005 Aug 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16511166 16511166]
+The structure at 2.5 A resolution of human basophilic leukemia-expressed protein BLES03., Bitto E, Bingman CA, Robinson H, Allard ST, Wesenberg GE, Phillips GN Jr, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Sep 1;61(Pt, 9):812-7. Epub 2005 Aug 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16511166 16511166]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Allard, S.T.M.]]
+[[Category: Allard, S T.M.]]
-[[Category: Bingman, C.A.]]
+[[Category: Bingman, C A.]]
 [[Category: Bitto, E.]]
-[[Category: CESG, Center.for.Eukaryotic.Structural.Genomics.]]
+[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
-[[Category: Jr., G.N.Phillips.]]
+[[Category: Jr., G N.Phillips.]]
-[[Category: Wesenberg, G.E.]]
+[[Category: Wesenberg, G E.]]
 [[Category: bc010512]]
 [[Category: bles03]]
 [[Category: center for eukaryotic structural genomics]]
 [[Category: cesg]]
-[[Category: hs.433573]]
+[[Category: hs 433573]]
 [[Category: p5326]]
 [[Category: protein structure initiative]]
@@ Line 30: / Line 30: @@
 [[Category: unknown function]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:16:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:18:58 2008''