1ztp: Difference between revisions

Revision as of 08:18, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ztp.png

Template:STRUCTURE 1ztp

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

Template:ABSTRACT PUBMED 16511166

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 Mon Jul 28 08:18:06 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ztp.gif|left|200px]]
+{{Seed}}
+[[Image:1ztp.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ztp|  PDB=1ztp  |  SCENE=  }}
-'''X-ray structure of gene product from homo sapiens Hs.433573'''
+===X-ray structure of gene product from homo sapiens Hs.433573===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_16511166}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16511166 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16511166}}
 ==About this Structure==
@@ Line 38: / Line 42: @@
 [[Category: Structural genomic]]
 [[Category: Unknown function]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:03:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:18:06 2008''