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The structural flexibility of the shank1 PDZ domain is important for its binding to different ligands

Cited 7 time in scopus
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Title
The structural flexibility of the shank1 PDZ domain is important for its binding to different ligands
Other Titles
shank1 PDZ domain의 구조적인 변화가 다른 결합 단백질과의 상호작용에 중요
Authors
Soo Jeong Park
Soo Hyun Eom
HaJeung Park
Lee, Jun Hyuck
Kim, Hak Jun
Subject
Biochemistry & Molecular Biology; Biophysics
Keywords
GKAP; PDZ; Rattus norvegicus; Shank; βPIX
Issue Date
2011
Publisher
elsevier
Citation
Soo Jeong Park, et al. 2011. "The structural flexibility of the shank1 PDZ domain is important for its binding to different ligands". Biochemical and Biophysical Research Communications, 407(1): 207-212.
Abstract
The PDZ domain of the shank protein interacts with numerous cell membrane receptors and cytosolic proteins via the loosely defined binding motif X-(Ser/Thr)-X-Φ-COOH (Φ represents hydrophobic residues) at the carboxyl terminus of its target protein. This enables shank to serve as a membrane-associated scaffold for the assembly of signaling complexes. As the list of proteins that bind to the shank PDZ domain grows, it is not immediately clear what structural element(s) mediate this domain’s target specificity or the plasticity required to bind its different targets. Here, we have determined the crystal structure of the shank1 PDZ in complex with the βPIX C-terminal pentapeptide (642-646, DETNL) at 2.3 ?resolution and modeled shank1 PDZ binding to selected pentapeptide ligands.Overall, our study provides a new level of understanding of the specificity and structural plasticity of the shank PDZ domain.target protein. This enables shank to serve as a membrane-associated scaffold for the assembly of signaling complexes. As the list of proteins that bind to the shank PDZ domain grows, it is not immediately clear what structural element(s) mediate this domain’s target specificity or the plasticity required to bind its different targets. Here, we have determined the crystal structure of the shank1 PDZ in complex with the βPIX C-terminal pentapeptide (642-646, DETNL) at 2.3 ?resolution and modeled shank1 PDZ binding to selected pentapeptide ligands.Overall, our study provides a new level of understanding of the specificity and structural plasticity of the shank PDZ domain.
URI
http://repository.kopri.re.kr/handle/201206/5703
DOI
http://dx.doi.org/10.1016/j.bbrc.2011.02.141
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