PDBsum entry 3fe3

Transferase

PDB id: 3fe3

Contents

Protein chains

317 a.a.

Waters ×398

References listed in PDB file

Key reference

Title

Crystal structure of the kinase mark3/par-1: t211a-S215a double mutant

Authors

C.Nugoor, A.Marx, S.Panneerselvam, E.-M.Mandelkow, E.Mandelkow.

Ref.

TO BE PUBLISHED ...

Secondary reference #1

Title

Structure of the catalytic and ubiquitin-Associated domains of the protein kinase mark/par-1.

Authors

S.Panneerselvam, A.Marx, E.M.Mandelkow, E.Mandelkow.

Ref.

Structure, 2006, 14, 173-183. [DOI no: 10.1016/j.str.2005.09.022]

PubMed id

16472737

Figure 7.
Figure 7. Common Docking Domain and ED Site of MAP Kinases Compared to MARK2
The structures of (A) MARK2 and (B) ERK2 (PDB code 2ERK [Canagarajah et al., 1997]) are shown in the same orientations after least-squares superposition of 35 residues from helix E to the catalytic loop. The common docking domain (CD, in red) according to Tanoue and Nishida (2003) is C terminal to the kinase domain and corresponds in MARK to the first half of the tether connecting the kinase domain to the UBA domain (residues vert, similar 305-315). The C-terminal extensions following the CD domain (linker and UBA domain in MARK2) are shown in purple. Characteristic for the CD domain is a cluster of negatively charged residues exposed to the surface, located in a bulge at the end of the catalytic domain (stick model representation).

The above figure is reproduced from the cited reference with permission from Cell Press

Secondary reference #2

Title

Structural variations in the catalytic and ubiquitin-Associated domains of microtubule-Associated protein/microtubule affinity regulating kinase (mark) 1 and mark2.

Authors

A.Marx, C.Nugoor, J.Müller, S.Panneerselvam, T.Timm, M.Bilang, E.Mylonas, D.I.Svergun, E.M.Mandelkow, E.Mandelkow.

Ref.

J Biol Chem, 2006, 281, 27586-27599. [DOI no: 10.1074/jbc.M604865200]

PubMed id

16803889

Figure 5.
FIGURE 5. MARK2 dimer compared with MARK1 molecules E and F. a, overlay of the MARK2 dimer (red) and molecules E and F of MARK2 (green). b, close-up view of the activation segment (magenta) and the surrounding elements in molecule E of MARK1 (dark colors), with nearby elements of molecule F shown in pale colors. c, asin b but with molecule F (dark colors) in the same orientation as molecule E in panel b; pale colors are for elements belonging to molecule E. All superpositions by fit of the C-lobes using helices E and F as reference structures. Similar interactions as between molecules E/F exist between MARK1 molecules A/B, C/D, and G/H.

Figure 9.
FIGURE 9. Inhibition by extra-catalytic domains in c-Src and MARK. Catalytic domains are in blue with activation segments (ASeg) in yellow; hinge regions are marked by white circles. All molecules are shown in the same orientation as determined by least squares fitting of helices E and F of the C-lobes. a, restrained (inactive) conformation of human c-Src (PDB code 2SRC (38)). The SH3 and SH2 domains of c-Src are N-terminal to the catalytic domain. The SH3 domain and the linker between SH2 and catalytic domain bind together to the N-lobe and are shown in the same color (red). The SH2 domain binds to the tail of the catalytic domain via interaction with phosphotyrosine Tyr-527. The connector between the SH3 and the SH2 domain (lock, shown in green) is essential for inhibition of c-Src as it efficiently restricts breathing movements of the catalytic domain (36). b, MARK, represented by molecule E of the MARK1 crystal structure. c, hypothetical active conformation of MARK, with activation segment and orientation of the N-lobe (and UBA domain) relative to the C-lobe modeled by comparison with Aurora A, active conformation (PDB code 1OL5 (41)). Rotation of the UBA domain in synchrony with the N-lobe is accomplished by unfolding the base of the linker (labeled CD in analogy to CD domains of MAP kinases (42)). According to this model, efficient damping of the catalytic domain breathing movements requires stabilization of the CD domain by binding of another interaction partner.

The above figures are reproduced from the cited reference with permission from the ASBMB