Journal article icon

Journal article

Structural analysis of the interactions between paxillin LD motifs and alpha-parvin.

Abstract:

The adaptor protein paxillin contains five conserved leucine-rich (LD) motifs that interact with a variety of focal adhesion proteins, such as alpha-parvin. Here, we report the first crystal structure of the C-terminal calponin homology domain (CH(C)) of alpha-parvin at 1.05 A resolution and show that it is able to bind all the LD motifs, with some selectivity for LD1, LD2, and LD4. Cocrystal structures with these LD motifs reveal the molecular details of their interactions with a common bind...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1016/j.str.2008.08.007

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Campbell, ID More by this author
Expand authors...
Journal:
Structure (London, England : 1993)
Volume:
16
Issue:
10
Pages:
1521-1531
Publication date:
2008-10-05
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:54984273-aa6c-4e87-97ba-e240f47332f9
Source identifiers:
99827
Local pid:
pubs:99827

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP