PDBsum entry: 3e2u

Protein binding

PDB-id: 3e2u

Contents

Description

Header details

Header records

References

PROCHECK

Protein chains

71 a.a. *

23 a.a. *

24 a.a. *

Metal ions

_ZN ×4

Waters ×58

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

3e2u

Name:

Protein binding

Title:

Crystal structure of the zink-knuckle 2 domain of human clip-170 in complex with cap-gly domain of human dynactin- 1 (p150-glued)

Structure:

Dynactin subunit 1. Chain: a, b, c, d. Fragment: cap-gly domain. Synonym: 150 kda dynein-associated polypeptide, dap-150, dp-150, p150-glued, p135. Engineered: yes. Cap-gly domain-containing linker protein 1. Chain: e, f, g, h. Fragment: zn-knuckle 2.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dctn1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: clip1, cyln1, rsn.

UniProt:

Chains A, B, C, D: Q14203 (DCTN1_HUMAN)

Seq:
Struc:
	Seq:
	Struc:
Seq:
Struc:
	Seq:
	Struc:
Seq:
Struc:
	Seq:	1278 a.a.
	Struc:	71 a.a.

Chains E, F: P30622 (CLIP1_HUMAN)

Seq:
Struc:
	Seq:
	Struc:
Seq:
Struc:
	Seq:
	Struc:
Seq:
Struc:
	Seq:	1438 a.a.
	Struc:	23 a.a.

Chains G, H: P30622 (CLIP1_HUMAN)

Seq:

Struc:

Seq:

Struc:

Seq:

Struc:

Seq:

Struc:

Seq:

Struc:

Seq:

1438 a.a.

Struc:

24 a.a.

Key:	PfamA domain	PfamB domain
Secondary structure

Resolution:

2.60Å

R-factor:

0.193

R-free:

0.238

Authors:

A.Weisbrich,S.Honnappa,G.Capitani,M.O.Steinmetz

Key ref:

A.Weisbrich et al. (2007). Structure-function relationship of CAP-Gly domains.. Nat Struct Biol, 14, 959-967. [PubMed id: 17828277] [DOI: 10.1038/nsmb1291]

Date:

06-Aug-08

Release date:

19-Aug-08

Supersedes:

2pzo

Related entries:

2cp5
solution structure of the 1st cap-gly domain in human clip-
170/restin
2hkn
crystal structure of the cap-gly domain of human dynactin-1
(p150-glued)
2hkq
crystal structure of thE C-terminal domain of human eb1 in
complex with the cap-gly domain of human dynactin-1 (p150-
glued)
... plus others (see Header records)

Quick_links

Procheck

Surface

Key reference

DOI no: 10.1038/nsmb1291

Nat Struct Biol 14:959-967 (2007)

PubMed id: 17828277

Structure-function relationship of CAP-Gly domains.

A.Weisbrich, S.Honnappa, R.Jaussi, O.Okhrimenko, D.Frey, I.Jelesarov, A.Akhmanova, M.O.Steinmetz.

ABSTRACT

In all eukaryotes, CAP-Gly proteins control important cellular processes. The molecular mechanisms underlying the functions of CAP-Gly domains, however, are still poorly understood. Here we use the complex formed between the CAP-Gly domain of p150(glued) and the C-terminal zinc knuckle of CLIP170 as a model system to explore the structure-function relationship of CAP-Gly-mediated protein interactions. We demonstrate that the conserved GKNDG motif of CAP-Gly domains is responsible for targeting to the C-terminal EEY/F sequence motifs of CLIP170, EB proteins and microtubules. The CAP-Gly-EEY/F interaction is essential for the recruitment of the dynactin complex by CLIP170 and for activation of CLIP170. Our findings define the molecular basis of CAP-Gly domain function, including the tubulin detyrosination-tyrosination cycle. They further establish fundamental roles for the interaction between CAP-Gly proteins and C-terminal EEY/F sequence motifs in regulating complex and dynamic cellular processes.

Selected figure(s)

Figure 4.
(a–e) COS-7 cells were transfected with constructs expressing YFP or the indicated fluorescent CLIP170 fusions and stained for endogenous p150^glued. Schematic representations of CLIP170 fusions are shown at left; CAP-Gly domains (CG1, CG2), zinc knuckles (Zn1, Zn2), DDETF motif and coiled-coil region are indicated. Right images show overlays of YFP fluorescence (green) and staining of endogenous p150^glued (magenta). Inset in the middle panel in a shows an enlargement of the boxed area to illustrate localization of p150^glued to microtubule tips in control cells. Bar, 10 m.

Figure 7.
Olive, orange and blue double arrows represent interactions mediated by CLIP170 CAP-Gly, p150^glued CAP-Gly and the calponin-homology (CH) domain of EB1, respectively. Dashed and solid lines denote intra- and intermolecular interactions, respectively. Note that EB1, CLIP170 and p150^glued form parallel dimers; however, for simplicity only the monomers are depicted.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2007, 14, 959-967) copyright 2007.

Figures were selected by the author.