Structure of human DPEP3 in complex with the SC-003 antibody Fab fragment reveals basis for lack of dipeptidase activity

Hayashi, Kristyn; Longenecker, Kenton L.; Koenig, Patrick; Prashar, Aditi; Hampl, Johannes; Stoll, Vincent; Vivona, Sandro

doi:10.1016/j.jsb.2020.107512

Title: Structure of human DPEP3 in complex with the SC-003 antibody Fab fragment reveals basis for lack of dipeptidase activity

Full Record
Other Related Research

Authors:: Hayashi, Kristyn; Longenecker, Kenton L.; Koenig, Patrick; Prashar, Aditi; Hampl, Johannes; Stoll, Vincent; Vivona, Sandro

Publication Date:: Wed Jul 01 00:00:00 EDT 2020

Sponsoring Org.:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

OSTI Identifier:: 1630366

Grant/Contract Number:: AC02-06CH11357

Resource Type:: Published Article

Journal Name:: Journal of Structural Biology

Additional Journal Information:: Journal Name: Journal of Structural Biology Journal Volume: 211 Journal Issue: 1; Journal ID: ISSN 1047-8477

Publisher:: Elsevier

Country of Publication:: United States

Language:: English

Citation Formats


                    Hayashi, Kristyn, Longenecker, Kenton L., Koenig, Patrick, Prashar, Aditi, Hampl, Johannes, Stoll, Vincent, and Vivona, Sandro. Structure of human DPEP3 in complex with the SC-003 antibody Fab fragment reveals basis for lack of dipeptidase activity.  United States: N. p., 2020. 
Web.  doi:10.1016/j.jsb.2020.107512.

Copy to clipboard


                    Hayashi, Kristyn, Longenecker, Kenton L., Koenig, Patrick, Prashar, Aditi, Hampl, Johannes, Stoll, Vincent, & Vivona, Sandro. Structure of human DPEP3 in complex with the SC-003 antibody Fab fragment reveals basis for lack of dipeptidase activity.  United States.  https://doi.org/10.1016/j.jsb.2020.107512

Copy to clipboard


                    Hayashi, Kristyn, Longenecker, Kenton L., Koenig, Patrick, Prashar, Aditi, Hampl, Johannes, Stoll, Vincent, and Vivona, Sandro. Wed .  
"Structure of human DPEP3 in complex with the SC-003 antibody Fab fragment reveals basis for lack of dipeptidase activity".  United States.  https://doi.org/10.1016/j.jsb.2020.107512.

Copy to clipboard


                    
@article{osti_1630366,

  title        = {Structure of human DPEP3 in complex with the SC-003 antibody Fab fragment reveals basis for lack of dipeptidase activity},

  author       = {Hayashi, Kristyn and Longenecker, Kenton L. and Koenig, Patrick and Prashar, Aditi and Hampl, Johannes and Stoll, Vincent and Vivona, Sandro},

  abstractNote = {},

  doi          = {10.1016/j.jsb.2020.107512},

  journal      = {Journal of Structural Biology},

  number       = 1,

  volume       = 211,

  place        = {United States},

  year         = {Wed Jul 01 00:00:00 EDT 2020},

  month        = {Wed Jul 01 00:00:00 EDT 2020}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Publisher's Version of Record
https://doi.org/10.1016/j.jsb.2020.107512

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 3 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:

Structure of human DPEP3 in complex with the SC-003 antibody Fab fragment reveals basis for lack of dipeptidase activity

Journal Article Hayashi, Kristyn ; Longenecker, Kenton L. ; Koenig, Patrick ; ... - J. Struct. Biol.
https://doi.org/10.1016/j.jsb.2020.107512
Atomic Basis for the Species-specific Inhibition of [alpha]V Integrins by Monoclonal Antibody 17E6 Is Revealed by the Crystal Structure of [alpha]V[beta]3 Ectodomain-17E6 Fab Complex

Journal Article Mahalingam, Bhuvaneshwari ; Agthoven, Johannes F.Van ; Xiong, Jian-Ping ; ... - J. Biol. Chem.
https://doi.org/10.1074/jbc.M113.546929
Complex of human Melanotransferrin and SC57.32 Fab fragment reveals novel interdomain arrangement with ferric N-lobe and open C-lobe

Journal Article Hayashi, Kristyn ; Longenecker, Kenton L. ; Liu, Yi-Liang ; ... - Scientific Reports

AbstractMelanotransferrin (MTf) is an iron-binding member of the transferrin superfamily that can be membrane-anchored or secreted in serum. On cells, it can mediate transferrin-independent iron uptake and promote proliferation. In serum, it is a transcytotic iron transporter across the blood–brain barrier. MTf has been exploited as a drug delivery carrier to the brain and as an antibody-drug conjugate (ADC) target due to its oncogenic role in melanoma and its elevated expression in triple-negative breast cancer (TNBC). For treatment of TNBC, an MTf-targeting ADC completed a phase I clinical trial (NCT03316794). The structure of its murine, unconjugated Fab fragment (SC57.32) is revealedmore »« less
https://doi.org/10.1038/s41598-020-79090-8

Full Text Available
Detection of immune complexes using $sup 125$I goat anti(human IgG) monovalent (Fab) antibody fragments

Journal Article Ludwig, F J ; Cusumanoo, C L - J. Nat. Cancer Inst., v. 52, no. 5, pp. 1529-1536
Potent neutralization of VEGF biological activities with a fully human antibody Fab fragment directed against VEGF receptor 2

Journal Article Miao, H -Q ; Hu, Kun ; Jimenez, Xenia ; ... - Biochemical and Biophysical Research Communications

Compelling evidence suggest that vascular endothelial growth factor (VEGF) and its receptors, especially receptor 2 (VEGFR2, or kinase insert domain-containing receptor, KDR), play a critical role in angiogenesis under both physiological and pathological conditions, including cancer and angiogenic retinopathies such as age-related macular degeneration (AMD). To this end, inhibition of angiogenesis with antagonists to either VEGF or KDR has yielded significant therapeutic efficacy both in preclinical studies in animal models and in clinical trials in patients with cancer and AMD. We previously reported the identification of a high affinity, fully human anti-KDR antibody fragment, 1121B Fab, through a highly stringentmore »« less
https://doi.org/10.1016/j.bbrc.2006.04.119

Similar Records