Structural basis for the binding of the cancer targeting scorpion toxin, ClTx, to the vascular endothelia growth factor receptor neuropilin-1

Autor: Gagan Sharma, Carolyne B. Braga, Kai-En Chen, Xinying Jia, Venkatraman Ramanujam, Brett M. Collins, Roberto Rittner, Mehdi Mobli

Publikováno v: Current Research in Structural Biology, Vol 3, Iss , Pp 179-186 (2021)

Chlorotoxin (ClTx) is a 36-residue disulfide-rich peptide isolated from the venom of the scorpion Leiurus quinquestriatus. This peptide has been shown to selectively bind to brain tumours (gliomas), however, with conflicting reports regarding its dir

Externí odkaz: https://doaj.org/article/af52d3404ddf4994b4ff881afbc923be

Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities

Autor: Mintu Chandra, Yanni K.-Y. Chin, Caroline Mas, J. Ryan Feathers, Blessy Paul, Sanchari Datta, Kai-En Chen, Xinying Jia, Zhe Yang, Suzanne J. Norwood, Biswaranjan Mohanty, Andrea Bugarcic, Rohan D. Teasdale, W. Mike Henne, Mehdi Mobli, Brett M. Collins

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)

Phox homology (PX) domains are membrane interacting domains that bind to various lipids. Here authors screen all human PX domains systematically for their phospholipid preferences and define four classes and provide the basis for defining and predict

Externí odkaz: https://doaj.org/article/837519800813434db7bd127742edba4b

Interaction between plate make and protein in protein crystallisation screening.

Autor: Gordon J King, Kai-En Chen, Gautier Robin, Jade K Forwood, Begoña Heras, Anil S Thakur, Bostjan Kobe, Simon P Blomberg, Jennifer L Martin

Publikováno v: PLoS ONE, Vol 4, Iss 11, p e7851 (2009)

Protein crystallisation screening involves the parallel testing of large numbers of candidate conditions with the aim of identifying conditions suitable as a starting point for the production of diffraction quality crystals. Generally, condition scre

Externí odkaz: https://doaj.org/article/008bf3fc0f97499fbc81c20ef64faf36

Structure of the Commander Endosomal Trafficking Complex Linked to X-Linked Intellectual Disability/Ritscher-Schinzel Syndrome

Autor: Michael D. Healy, Kerrie E. McNally, Rebeka Butkovic, Molly Chilton, Kohji Kato, Joanna Sacharz, Calum McConville, Edmund R.R. Moody, Shrestha Shaw, Vicente J. Planelles-Herrero, Sathish K.N. Yadav, Jennifer Ross, Ufuk Borucu, Catherine S. Palmer, Kai-En Chen, Tristan I. Croll, Ryan J. Hall, Nikeisha J. Caruana, Rajesh Ghai, Thi H.D. Nguyen, Kate J. Heesom, Shinji Saitoh, Imre Berger, Christiane Schaffitzel, Tom A. Williams, David A. Stroud, Emmanuel Derivery, Brett M. Collins, Peter J. Cullen

SUMMARYThe Commander complex is required for endosomal recycling of diverse transmembrane cargos and is mutated in Ritscher-Schinzel syndrome. It comprises two subassemblies; Retriever composed of VPS35L, VPS26C and VPS29, and the CCC complex which c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23d210a5342199c943249b9d1af8c0d6
https://doi.org/10.2139/ssrn.4330804

SNX27-Retromer directly binds ESCPE-1 to transfer cargo proteins during endosomal recycling

Autor: Boris Simonetti, Qian Guo, Manuel Giménez-Andrés, Kai-En Chen, Edmund R. R. Moody, Ashley J. Evans, Mintu Chandra, Chris M. Danson, Tom A. Williams, Brett M. Collins, Peter J. Cullen

Publikováno v: Simonetti, B, Guo, Q, Gimenez Andres, M, Chen, K E, Moody, E R R, Evans, A J, Chandra, M, Danson, C M, Williams, T, Collins, B M & Cullen, P J 2022, ' SNX27–Retromer directly binds ESCPE-1 to transfer cargo proteins during endosomal recycling ', PLoS Biology, vol. 20, no. 4, e3001601 . https://doi.org/10.1371/journal.pbio.3001601

Coat complexes coordinate cargo recognition through cargo adaptors with biogenesis of transport carriers during integral membrane protein trafficking. Here, we combine biochemical, structural, and cellular analyses to establish the mechanistic basis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4737fd4aa6267f0f63f2c7711c5738f6
https://pubmed.ncbi.nlm.nih.gov/35417450