This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1g9l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
We have determined the solution structure of the C-terminal quarter of, human poly(A)-binding protein (hPABP). The protein fragment contains a, protein domain, PABC [for poly(A)-binding protein C-terminal domain], which is also found associated with the HECT family of ubiquitin ligases., By using peptides derived from PABP interacting protein (Paip) 1, Paip2, and eRF3, we show that PABC functions as a peptide binding domain. We use, chemical shift perturbation analysis to identify the peptide binding site, in PABC and the major elements involved in peptide recognition. From, comparative sequence analysis of PABC-binding peptides, we formulate a, preliminary PABC consensus sequence and identify human ataxin-2, the, protein responsible for type 2 spinocerebellar ataxia (SCA2), as a, potential PABC ligand.
+
We have determined the solution structure of the C-terminal quarter of human poly(A)-binding protein (hPABP). The protein fragment contains a protein domain, PABC [for poly(A)-binding protein C-terminal domain], which is also found associated with the HECT family of ubiquitin ligases. By using peptides derived from PABP interacting protein (Paip) 1, Paip2, and eRF3, we show that PABC functions as a peptide binding domain. We use chemical shift perturbation analysis to identify the peptide binding site in PABC and the major elements involved in peptide recognition. From comparative sequence analysis of PABC-binding peptides, we formulate a preliminary PABC consensus sequence and identify human ataxin-2, the protein responsible for type 2 spinocerebellar ataxia (SCA2), as a potential PABC ligand.
==About this Structure==
==About this Structure==
Line 18: Line 18:
[[Category: Khaleghpour, K.]]
[[Category: Khaleghpour, K.]]
[[Category: Kozlov, G.]]
[[Category: Kozlov, G.]]
-
[[Category: Trempe, J.F.]]
+
[[Category: Trempe, J F.]]
[[Category: all-helical domain]]
[[Category: all-helical domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:51:46 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:40 2008''

Revision as of 10:47, 21 February 2008


1g9l

Drag the structure with the mouse to rotate

SOLUTION STRUCTURE OF THE PABC DOMAIN OF HUMAN POLY(A) BINDING PROTEIN

Overview

We have determined the solution structure of the C-terminal quarter of human poly(A)-binding protein (hPABP). The protein fragment contains a protein domain, PABC [for poly(A)-binding protein C-terminal domain], which is also found associated with the HECT family of ubiquitin ligases. By using peptides derived from PABP interacting protein (Paip) 1, Paip2, and eRF3, we show that PABC functions as a peptide binding domain. We use chemical shift perturbation analysis to identify the peptide binding site in PABC and the major elements involved in peptide recognition. From comparative sequence analysis of PABC-binding peptides, we formulate a preliminary PABC consensus sequence and identify human ataxin-2, the protein responsible for type 2 spinocerebellar ataxia (SCA2), as a potential PABC ligand.

About this Structure

1G9L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure and function of the C-terminal PABC domain of human poly(A)-binding protein., Kozlov G, Trempe JF, Khaleghpour K, Kahvejian A, Ekiel I, Gehring K, Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4409-13. Epub 2001 Apr 3. PMID:11287632

Page seeded by OCA on Thu Feb 21 12:47:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools