PfSec13 is a structural homolog of ScSec13·Nup145C.

Slides:

Advertisements

Similar presentations

Envelope generated by the interaction of the EODs of three weakly electric fish. Envelope generated by the interaction of the EODs of three weakly electric.

Advertisements

Volume 13, Issue 10, Pages (October 2006)

Ross Alexander Robinson, Xin Lu, Edith Yvonne Jones, Christian Siebold

Volume 15, Issue 11, Pages (November 2007)

Sebastian Meyer, Raimund Dutzler Structure

Structure of an LDLR-RAP Complex Reveals a General Mode for Ligand Recognition by Lipoprotein Receptors Carl Fisher, Natalia Beglova, Stephen C. Blacklow

Volume 25, Issue 11, Pages e2 (November 2017)

Molecular Basis of Box C/D RNA-Protein Interactions

Tom Huxford, De-Bin Huang, Shiva Malek, Gourisankar Ghosh Cell

Volume 108, Issue 6, Pages (March 2002)

Volume 99, Issue 1, Pages (October 1999)

Volume 13, Issue 10, Pages (October 2006)

Volume 25, Issue 1, Pages (January 2017)

Ross Alexander Robinson, Xin Lu, Edith Yvonne Jones, Christian Siebold

Volume 4, Issue 5, Pages (November 1999)

Jason O. Moore, Wayne A. Hendrickson Structure

The Crystal Structure of the Costimulatory OX40-OX40L Complex

Error-Prone DNA Polymerases

Sequence alignment of PHCCEx domains with secondary structure elements of the Tiam2 PHCCEx domain at the top. Sequence alignment of PHCCEx domains with.

Volume 23, Issue 3, Pages (August 2006)

Volume 3, Issue 4, Pages (April 1999)

Crystal Structure of the N-Terminal Domain of the Secretin GspD from ETEC Determined with the Assistance of a Nanobody Konstantin V. Korotkov, Els Pardon,

Jason O. Moore, Wayne A. Hendrickson Structure

The Unmasking of Telomerase

Volume 13, Issue 7, Pages (July 2005)

Cell Signalling: Receptor orphans find a family

Crystal Structures of the BAR-PH and PTB Domains of Human APPL1

Meigang Gu, Kanagalaghatta R. Rajashankar, Christopher D. Lima

Bioinformatics analysis of the small TbTim amino acid sequences.

Jeffrey J. Wilson, Rhett A. Kovall Cell

Sequence conservation across the Ub-binding sites of human USPs

Multiple sequence alignment of STAT6 and other STAT proteins produced by ClusterW and ESpript (espript.ibcp.fr/ESPript/ESPript/). Multiple sequence alignment.

Volume 5, Issue 10, Pages (October 1997)

The RC4 Domain of PbrS-RNase Is Critical for Interaction with PbrActin1. The RC4 Domain of PbrS-RNase Is Critical for Interaction with PbrActin1. (A) Dissection.

Modeling tumor invasion in the Drosophila larval wing disc.

A highly conserved six-amino-acid region in the C-terminal CT domain of MARCH8 is responsible for its ability to downregulate TfR. A highly conserved six-amino-acid.

The C-terminal membrane-proximal region of MARCH8 interacts with TfR.

PfSec13 does not co-localize with P. falciparum heterochromatin.

Proteins associated with PfSec13.

Transcription factor network of human pancreas development.

Annoted amino acid sequence of Aedes aegypti gliotactin (Gli).

Fig. 4. The predicted protein domains in sma

Membrane and organelle dynamics.

Mosquito GluCl alignment and anti-AgGluCl IgG specificity.

Overview of HEAT-motif-containing proteins.

Example of a putative bridging fiber.

Alignment of the deduced amino acid sequences of the myosin light chain 2 (MLC2) proteins. Alignment of the deduced amino acid sequences of the myosin.

Crystal Structure of the Flagellar σ/Anti-σ Complex σ28/FlgM Reveals an Intact σ Factor in an Inactive Conformation Margareta K. Sorenson, Soumya S.

MCAK has an extended conformation on microtubules.

Fig. 2. RGD and KGD motifs in N. vectensis thrombospondins

Identification of a functional domain in MKL1_S that allows specific transcriptional activity. Identification of a functional domain in MKL1_S that allows.

Amino acid sequence alignment of Calliphora (Cv) and Drosophila (Dm) rhodopsins. Amino acid sequence alignment of Calliphora (Cv) and Drosophila (Dm) rhodopsins.

RAD51 interacts with SUMO-1 through its SIM

LC8 is structurally variable but conserved in sequence.

Comparison of the sequences of Fzo/Mfn and structure of mammalian Mfn2

WT MARCH8, but not the CS mutant, specifically ubiquitinates and downregulates TfR. WT MARCH8, but not the CS mutant, specifically ubiquitinates and downregulates.

Conservation of key sequence features and endocytic localisation in TbCALM. Conservation of key sequence features and endocytic localisation in TbCALM.

Membrane integration of the model constructs depends on protein sequence, not codon usage. Membrane integration of the model constructs depends on protein.

Architecture of a Coat for the Nuclear Pore Membrane

Structural insights based on chimeric Alp4-GCP2 analysis.

Different structural strategies for homophilic binding of insect and vertebrate E-cadherins through their ectodomains. Different structural strategies.

Phylogenetic analysis and domain structure of CALM proteins.

Brett K. Kaiser, Matthew C. Clifton, Betty W. Shen, Barry L. Stoddard

Volume 7, Issue 2, Pages R19-R23 (February 1999)

Predicted Amino Acid Sequence of the Tomato Cf-4 Protein (Thomas et al

Modeling of EGFR exon 20 insertions using the 3-dimensional structure of the EGFR kinase domain predicts different interactions with the erlotinib-binding.

Structural Switch of the γ Subunit in an Archaeal aIF2αγ Heterodimer

Crystal Structure of Escherichia coli RNase D, an Exoribonuclease Involved in Structured RNA Processing Yuhong Zuo, Yong Wang, Arun Malhotra Structure

S. moellendorffii BBI3 Is Predicted to Be a BBI Based on Sequence Similarity at the Inhibitory Motifs and Shared Primary Protein Architecture. S. moellendorffii.

Alignment of the Amino Acid Sequences of NCS and Other PR10/Bet v1 Proteins from Various Plant Species.Deduced amino acid sequences were aligned using.

Presentation transcript:

PfSec13 is a structural homolog of ScSec13·Nup145C. PfSec13 is a structural homolog of ScSec13·Nup145C. (A) Structure-based sequence alignment of PfSec13 with ScSec13 and Nup145C. Residue numbering for PfSec13 is on top of the alignment. Secondary structural elements of ScSec13 are shown below the alignment. The β-propeller forming domain is indicated by the black box and the homology to Nup145C in the green box. Insertions specific to PfSec13 are labeled as I1–I3. Strictly conserved residues are highlighted by red shading. Homologous residues are highlighted in red text. (B) Overlay of the PfSec13 in silico model (purple) with crystal structure of ScSec13 (yellow; PDB code 3JRO) and Nup145c (green; PDB code 3JRO). The crystal structure of Nup84 is indicated in red (PDB code 3JRO). Noa Dahan-Pasternak et al. J Cell Sci 2013;126:3055-3069 © 2013. Published by The Company of Biologists Ltd