PDBsum entry 2d9q

Signaling protein/cytokine

PDB id

2d9q

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Contents

			Protein chains

					168 a.a. *


					299 a.a. *

			Ligands

					NAG-NAG

			Waters ×14

* Residue conservation analysis

PDB id:

2d9q

Links

Name:

Signaling protein/cytokine

Title:

Crystal structure of the human gcsf-receptor signaling complex

Structure:

Csf3. Chain: a. Fragment: residues 1-174. Synonym: granulocyte colony stimulating factor, gcsf. Engineered: yes. Granulocyte colony-stimulating factor receptor. Chain: b. Fragment: ig-crh domain. Synonym: g-csf-r, cd114 antigen, gcsf-r.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.80Å

R-factor:

0.253

R-free:

0.284

Authors:

T.Tamada,R.Kuroki

Key ref:

T.Tamada et al. (2006). Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex. Proc Natl Acad Sci U S A, 103, 3135-3140. PubMed id: 16492764 DOI: 10.1073/pnas.0511264103

Date:

12-Dec-05

Release date:

07-Feb-06

PROCHECK

	Headers

	References

Protein chain

P09919 (CSF3_HUMAN) - Granulocyte colony-stimulating factor from Homo sapiens

Seq: Struc:					207 a.a. 168 a.a.

Protein chain

Q99062 (CSF3R_HUMAN) - Granulocyte colony-stimulating factor receptor from Homo sapiens

Seq: Struc:

Seq: Struc:					836 a.a. 299 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1073/pnas.0511264103	Proc Natl Acad Sci U S A 103:3135-3140 (2006)
PubMed id: 16492764

Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex.
T.Tamada, E.Honjo, Y.Maeda, T.Okamoto, M.Ishibashi, M.Tokunaga, R.Kuroki.

ABSTRACT

A crystal structure of the signaling complex between human granulocyte colony-stimulating factor (GCSF) and a ligand binding region of GCSF receptor (GCSF-R), has been determined to 2.8 A resolution. The GCSF:GCSF-R complex formed a 2:2 stoichiometry by means of a cross-over interaction between the Ig-like domains of GCSF-R and GCSF. The conformation of the complex is quite different from that between human GCSF and the cytokine receptor homologous domain of mouse GCSF-R, but similar to that of the IL-6/gp130 signaling complex. The Ig-like domain cross-over structure necessary for GCSF-R activation is consistent with previously reported thermodynamic and mutational analyses.

Selected figure(s)



	Figure 1. Fig. 1. Overall structure of the 2:2 complex between hGCSF and hGCSF-R (Ig–CRH domain). The GCSF molecules are colored in red and orange, and GCSF-R molecules are colored in green and cyan. Fig. 1 was prepared by the PYMOL Molecular Graphics System (DeLano Scientific, San Carlos, CA).		Figure 3. Fig. 3. Close-up view of the interface between ligand and receptor. (a) Site II. (b) Site III. Related residues of ligand–receptor binding are drawn as stick model. Figs. 3–5 were prepared by WEBLAB VIEWER LITE (Accelrys Inc., San Diego).

Figures were selected by the author.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20078425

S.Mirza, A.Walker, J.Chen, J.M.Murphy, and I.G.Young (2010).
The Ig-like domain of human GM-CSF receptor alpha plays a critical role in cytokine binding and receptor activation.

Biochem J, 426, 307-317.

19586918

T.Ito, S.Suzuki, S.Kanaji, H.Shiraishi, S.Ohta, K.Arima, G.Tanaka, T.Tamada, E.Honjo, K.C.Garcia, R.Kuroki, and K.Izuhara (2009).
Distinct structural requirements for interleukin-4 (IL-4) and IL-13 binding to the shared IL-13 receptor facilitate cellular tuning of cytokine responsiveness.

J Biol Chem, 284, 24289-24296.

18817510

X.Wang, P.Lupardus, S.L.Laporte, and K.C.Garcia (2009).
Structural biology of shared cytokine receptors.

Annu Rev Immunol, 27, 29-60.

18400509

A.D.Panopoulos, and S.S.Watowich (2008).
Granulocyte colony-stimulating factor: molecular mechanisms of action during steady state and 'emergency' hematopoiesis.

Cytokine, 42, 277-288.

18775332

G.Skiniotis, P.J.Lupardus, M.Martick, T.Walz, and K.C.Garcia (2008).
Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex.

Mol Cell, 31, 737-748.

PDB code:

3e0g

18250627

K.U.Wendt, M.S.Weiss, P.Cramer, and D.W.Heinz (2008).
Structures and diseases.

Nat Struct Mol Biol, 15, 117-120.

17586772

H.Yamada, T.Tamada, M.Kosaka, K.Miyata, S.Fujiki, M.Tano, M.Moriya, M.Yamanishi, E.Honjo, H.Tada, T.Ino, H.Yamaguchi, J.Futami, M.Seno, T.Nomoto, T.Hirata, M.Yoshimura, and R.Kuroki (2007).
'Crystal lattice engineering,' an approach to engineer protein crystal contacts by creating intermolecular symmetry: crystallization and structure determination of a mutant human RNase 1 with a hydrophobic interface of leucines.

Protein Sci, 16, 1389-1397.

PDB codes:

2e0j 2e0l 2e0m 2e0o

17934480

L.Robb (2007).
Cytokine receptors and hematopoietic differentiation.

Oncogene, 26, 6715-6723.

16822289

A.Khwaja (2006).
The role of Janus kinases in haemopoiesis and haematological malignancy.

Br J Haematol, 134, 366-384.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.