1cvj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1cvj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cvj, resolution 2.6&Aring;" /> '''X-RAY CRYSTAL STRUCT...)
Line 1: Line 1:
-
[[Image:1cvj.gif|left|200px]]<br />
+
[[Image:1cvj.gif|left|200px]]<br /><applet load="1cvj" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1cvj" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1cvj, resolution 2.6&Aring;" />
caption="1cvj, resolution 2.6&Aring;" />
'''X-RAY CRYSTAL STRUCTURE OF THE POLY(A)-BINDING PROTEIN IN COMPLEX WITH POLYADENYLATE RNA'''<br />
'''X-RAY CRYSTAL STRUCTURE OF THE POLY(A)-BINDING PROTEIN IN COMPLEX WITH POLYADENYLATE RNA'''<br />
==Overview==
==Overview==
-
The cocrystal structure of human poly(A)-binding protein (PABP) has been, determined at 2.6 A resolution. PABP recognizes the 3' mRNA poly(A) tail, and plays critical roles in eukaryotic translation initiation and mRNA, stabilization/degradation. The minimal PABP used in this study consists of, the N-terminal two RRM-type RNA-binding domains connected by a short, linker (RRM1/2). These two RRMs form a continuous RNA-binding trough, lined by an antiparallel beta sheet backed by four alpha helices. The, polyadenylate RNA adopts an extended conformation running the length of, the molecular trough. Adenine recognition is primarily mediated by, contacts with conserved residues found in the RNP motifs of the two RRMs., The convex dorsum of RRM1/2 displays a phylogenetically conserved, hydrophobic/acidic portion, which may interact with translation initiation, factors and regulatory proteins.
+
The cocrystal structure of human poly(A)-binding protein (PABP) has been determined at 2.6 A resolution. PABP recognizes the 3' mRNA poly(A) tail and plays critical roles in eukaryotic translation initiation and mRNA stabilization/degradation. The minimal PABP used in this study consists of the N-terminal two RRM-type RNA-binding domains connected by a short linker (RRM1/2). These two RRMs form a continuous RNA-binding trough, lined by an antiparallel beta sheet backed by four alpha helices. The polyadenylate RNA adopts an extended conformation running the length of the molecular trough. Adenine recognition is primarily mediated by contacts with conserved residues found in the RNP motifs of the two RRMs. The convex dorsum of RRM1/2 displays a phylogenetically conserved hydrophobic/acidic portion, which may interact with translation initiation factors and regulatory proteins.
==About this Structure==
==About this Structure==
-
1CVJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with A as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CVJ OCA].
+
1CVJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=A:'>A</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVJ OCA].
==Reference==
==Reference==
Line 14: Line 13:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Bonanno, J.B.]]
+
[[Category: Bonanno, J B.]]
-
[[Category: Burley, S.K.]]
+
[[Category: Burley, S K.]]
-
[[Category: Deo, R.C.]]
+
[[Category: Deo, R C.]]
[[Category: Sonenberg, N.]]
[[Category: Sonenberg, N.]]
[[Category: A]]
[[Category: A]]
Line 22: Line 21:
[[Category: rrm]]
[[Category: rrm]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:25:46 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:15 2008''

Revision as of 10:10, 21 February 2008


1cvj, resolution 2.6Å

Drag the structure with the mouse to rotate

X-RAY CRYSTAL STRUCTURE OF THE POLY(A)-BINDING PROTEIN IN COMPLEX WITH POLYADENYLATE RNA

Overview

The cocrystal structure of human poly(A)-binding protein (PABP) has been determined at 2.6 A resolution. PABP recognizes the 3' mRNA poly(A) tail and plays critical roles in eukaryotic translation initiation and mRNA stabilization/degradation. The minimal PABP used in this study consists of the N-terminal two RRM-type RNA-binding domains connected by a short linker (RRM1/2). These two RRMs form a continuous RNA-binding trough, lined by an antiparallel beta sheet backed by four alpha helices. The polyadenylate RNA adopts an extended conformation running the length of the molecular trough. Adenine recognition is primarily mediated by contacts with conserved residues found in the RNP motifs of the two RRMs. The convex dorsum of RRM1/2 displays a phylogenetically conserved hydrophobic/acidic portion, which may interact with translation initiation factors and regulatory proteins.

About this Structure

1CVJ is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Recognition of polyadenylate RNA by the poly(A)-binding protein., Deo RC, Bonanno JB, Sonenberg N, Burley SK, Cell. 1999 Sep 17;98(6):835-45. PMID:10499800

Page seeded by OCA on Thu Feb 21 12:10:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools