Structures of C1q-like Proteins Reveal Unique Features among the C1q/TNF Superfamily

Ressl, Susanne; Vu, Brandon K.; Vivona, Sandro; Martinelli, David C.; Südhof, Thomas C.; Brunger, Axel T.

doi:10.1016/j.str.2015.01.019

Title: Structures of C1q-like Proteins Reveal Unique Features among the C1q/TNF Superfamily

Full Record
Other Related Research

Authors:: Ressl, Susanne; Vu, Brandon K.; Vivona, Sandro; Martinelli, David C.; Südhof, Thomas C.; Brunger, Axel T.

Publication Date:: Wed Apr 01 00:00:00 EDT 2015

Sponsoring Org.:: USDOE Office of Science (SC), Biological and Environmental Research (BER)

OSTI Identifier:: 1246529

Resource Type:: Published Article

Journal Name:: Structure

Additional Journal Information:: Journal Name: Structure Journal Volume: 23 Journal Issue: 4; Journal ID: ISSN 0969-2126

Publisher:: Elsevier

Country of Publication:: United Kingdom

Language:: English

Citation Formats


                    Ressl, Susanne, Vu, Brandon K., Vivona, Sandro, Martinelli, David C., Südhof, Thomas C., and Brunger, Axel T. Structures of C1q-like Proteins Reveal Unique Features among the C1q/TNF Superfamily.  United Kingdom: N. p., 2015. 
Web.  doi:10.1016/j.str.2015.01.019.

Copy to clipboard


                    Ressl, Susanne, Vu, Brandon K., Vivona, Sandro, Martinelli, David C., Südhof, Thomas C., & Brunger, Axel T. Structures of C1q-like Proteins Reveal Unique Features among the C1q/TNF Superfamily.  United Kingdom.  https://doi.org/10.1016/j.str.2015.01.019

Copy to clipboard


                    Ressl, Susanne, Vu, Brandon K., Vivona, Sandro, Martinelli, David C., Südhof, Thomas C., and Brunger, Axel T. Wed .  
"Structures of C1q-like Proteins Reveal Unique Features among the C1q/TNF Superfamily".  United Kingdom.  https://doi.org/10.1016/j.str.2015.01.019.

Copy to clipboard


                    
@article{osti_1246529,

  title        = {Structures of C1q-like Proteins Reveal Unique Features among the C1q/TNF Superfamily},

  author       = {Ressl, Susanne and Vu, Brandon K. and Vivona, Sandro and Martinelli, David C. and Südhof, Thomas C. and Brunger, Axel T.},

  abstractNote = {},

  doi          = {10.1016/j.str.2015.01.019},

  journal      = {Structure},

  number       = 4,

  volume       = 23,

  place        = {United Kingdom},

  year         = {Wed Apr 01 00:00:00 EDT 2015},

  month        = {Wed Apr 01 00:00:00 EDT 2015}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Publisher's Version of Record
https://doi.org/10.1016/j.str.2015.01.019

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 39 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

Structures of mouse and human GITR?GITRL complexes reveal unique TNF superfamily interactions

Journal Article Wang, Feng ; Chau, Bryant ; West, Sean M. ; ... - Nat. Commun.
https://doi.org/10.1038/s41467-021-21563-z
Human Suv3 protein reveals unique features among SF2 helicases

Journal Article Jedrzejczak, Robert ; Wang, Jiawei ; Dauter, Miroslawa ; ... - Acta Crystallogr. D

Suv3 is a helicase that is involved in efficient turnover and surveillance of RNA in eukaryotes. In vitro studies show that human Suv3 (hSuv3) in complex with human polynucleotide phosphorylase has RNA degradosome activity. The enzyme is mainly localized in mitochondria, but small fractions are found in cell nuclei. Here, two X-ray crystallographic structures of human Suv3 in complex with AMPPNP, a nonhydrolysable analog of ATP, and with a short five-nucleotide strand of RNA are presented at resolutions of 2.08 and 2.9 {angstrom}, respectively. The structure of the enzyme is very similar in the two complexes and consists of fourmore »« less
https://doi.org/10.1107/S0907444911040248
Human Suv3 protein reveals unique features among SF2 helicases

Journal Article Jedrzejczak, Robert ; Argonne National Laboratory, Argonne, IL 60439 ; Wang, Jiawei ; ... - Acta Crystallographica. Section D: Biological Crystallography

Crystal structures of the human mitochondrial helicase hSuv3 in complex with AMPPNP and with a short strand of RNA are presented. Suv3 is a helicase that is involved in efficient turnover and surveillance of RNA in eukaryotes. In vitro studies show that human Suv3 (hSuv3) in complex with human polynucleotide phosphorylase has RNA degradosome activity. The enzyme is mainly localized in mitochondria, but small fractions are found in cell nuclei. Here, two X-ray crystallographic structures of human Suv3 in complex with AMPPNP, a nonhydrolysable analog of ATP, and with a short five-nucleotide strand of RNA are presented at resolutions ofmore »« less
https://doi.org/10.1107/S0907444911040248
Evolution of GITRL Immune Function: Murine GITRL Exhibits Unique Structural and Biochemical Properties Within the TNF Superfamily

Journal Article Chattopadhyay, K ; Ramagopal, U ; Brenowitz, M ; ... - Proceedings of the National Academy of Sciences of the USA

Glucocorticoid-induced TNF receptor ligand (GITRL), a recently identified member of the TNF superfamily, binds to its receptor, GITR, on both effector and regulatory T cells and generates positive costimulatory signals implicated in a wide range of T cell functions. In contrast to all previously characterized homotrimeric TNF family members, the mouse GITRL crystal structure reveals a previously unrecognized dimeric assembly that is stabilized via a unique 'domain-swapping' interaction. Consistent with its crystal structure, mouse GITRL exists as a stable dimer in solution. Structure-guided mutagenesis studies confirmed the determinants responsible for dimerization and support a previously unrecognized receptor-recognition surface for mousemore »« less
https://doi.org/10.1073/pnas.0710529105
Comparative Analysis of the 15.5kD Box C/D snoRNP Core Protein in the Primitive Eukaryote Giardia lamblia Reveals Unique Structural and Functional Features

Journal Article Biswas, Shyamasri ; Buhrman, Greg ; Gagnon, Keith ; ... - Biochemistry-US

Box C/D ribonucleoproteins (RNP) guide the 2'-O-methylation of targeted nucleotides in archaeal and eukaryotic rRNAs. The archaeal L7Ae and eukaryotic 15.5kD box C/D RNP core protein homologues initiate RNP assembly by recognizing kink-turn (K-turn) motifs. The crystal structure of the 15.5kD core protein from the primitive eukaryote Giardia lamblia is described here to a resolution of 1.8 {angstrom}. The Giardia 15.5kD protein exhibits the typical {alpha}-{beta}-{alpha} sandwich fold exhibited by both archaeal L7Ae and eukaryotic 15.5kD proteins. Characteristic of eukaryotic homologues, the Giardia 15.5kD protein binds the K-turn motif but not the variant K-loop motif. The highly conserved residues ofmore »« less
https://doi.org/10.1021/bi1020474

Similar Records