Journal Article

PUBDB-2018-03870

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Probing the Architecture of a Multi-PDZ Domain Protein: Structure of PDZK1 in Solution

Hajizadeh, N. R. ; Pieprzyk, J.CSSB*EMBL* ; Skopintsev, P. ; Flayhan, A.CSSB*EMBL* ; Svergun, D. I. (Corresponding author)EMBL* ; Loew, C. (Corresponding author)CSSB*DESY*

2018
Elsevier Cambridge, Mass.

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Please use a persistent id in citations: doi:10.1016/j.str.2018.07.016

Abstract: The scaffolding protein PDZK1 has been associated with the regulation of membrane transporters. It contains four conserved PDZ domains, which typically recognize a 3–5-residue long motif at the C terminus of the binding partner. The atomic structures of the individual domains are available but their spatial arrangement in the full-length context influencing the binding properties remained elusive. Here we report a systematic study of full-length PDZK1 and deletion constructs using small-angle X-ray scattering, complemented with biochemical and functional studies on PDZK1 binding to known membrane protein partners. A hybrid modeling approach utilizing multiple scattering datasets yielded a well-defined, extended, asymmetric L-shaped domain organization of PDZK1 in contrast to a flexible “beads-on-string” model predicted by bioinformatics analysis. The linker regions of PDZK1 appear to play a central role in the arrangement of the four domains underlying the importance of studying scaffolding proteins in their full-length context.

Note: © Elsevier Ltd.; Post referee fulltext in progress; Embargo 12 months from publication

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Contributing Institute(s):

1. CSSB-EMBL (CSSB-EMBL)
2. EMBL (EMBL)
3. CSSB-EMBL-CL (CSSB-EMBL-CL)

Research Program(s):

1. 6G3 - PETRA III (POF3-622) (POF3-622)
2. SWEDEN-DESY - SWEDEN-DESY Collaboration (2020_Join2-SWEDEN-DESY) (2020_Join2-SWEDEN-DESY)

Experiment(s):

1. PETRA Beamline P12 (PETRA III)

Appears in the scientific report 2018

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Database coverage:
; BIOSIS Previews ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Ebsco Academic Search ; NCBI Molecular Biology Database ; Nationallizenz ; No Authors Fulltext ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

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