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PDBsum entry 1msh
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protein Protein-protein interface(s) links
Cytokine (chemotactic) PDB id
1msh

 

 

 

 

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Contents
Protein chain
72 a.a. *
* Residue conservation analysis
PDB id:
1msh
Name: Cytokine (chemotactic)
Title: Solution structure of gro(slash)melanoma growth stimulatory activity determined by 1h nmr spectroscopy
Structure: Human melanoma growth stimulatory activity. Chain: a, b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
NMR struc: 30 models
Authors: K.-S.Kim,I.Clark-Lewis,B.D.Sykes
Key ref: K.S.Kim et al. (1994). Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy. J Biol Chem, 269, 32909-32915. PubMed id: 7806518
Date:
25-Jan-95     Release date:   31-Mar-95    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P09341  (GROA_HUMAN) -  Growth-regulated alpha protein from Homo sapiens
Seq:
Struc: 		107 a.a.
72 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
J Biol Chem 269:32909-32915 (1994)
PubMed id: 7806518  
 
 
Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy.
K.S.Kim, I.Clark-Lewis, B.D.Sykes.
 
  ABSTRACT  
 
The three-dimensional solution structure of the growth-related protein-alpha/melanoma growth stimulatory activity (GRO/MGSA) has been solved by two-dimensional 1H nuclear magnetic resonance spectroscopy. The GRO/MGSA monomer consists of an NH2-terminal loop, a three-stranded antiparallel beta-sheet, and a COOH-terminal alpha-helix. Dimerization, which is apparent under the experimental conditions used (2 mM, pH 5.10, 30 degrees C), results in a six-stranded antiparallel beta-sheet and a pair of helices with 2-fold symmetry. While the basic fold is similar to that seen for interleukin-8 (IL-8) (Clore, G. M., Appella, E., Yamada, M., Matsushima, K., and Gronenborn, A. M. (1990) Biochemistry, 29, 1689-1696), there are differences in the ELR motif (residues 6-8), the turn involving residues 31-36, which is linked to the NH2-terminal region through the 9-35 disulfide bond. The most significant differences are in the NH2-terminal loop (residues 12-23). In IL-8, all the corresponding regions have been shown to be required for receptor binding (Clark-Lewis, I., Dewald, B., Loetscher, M., Moser, B., and Baggiolini, M. (1994) J. Biol. Chem. 269, 16075-16081). The structural differences thus have been identified between GRO/MGSA and IL-8 could contribute to their different receptor binding specificities.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19048342 Z.Cai, C.Gao, Y.Zhang, and K.Xing (2009).
Functional characterization of the ELR motif in piscine ELR+CXC-like chemokine.
  Mar Biotechnol (NY), 11, 505-512.  
17024562 L.Rajagopalan, and K.Rajarathnam (2006).
Structural basis of chemokine receptor function--a model for binding affinity and ligand selectivity.
  Biosci Rep, 26, 325-339.  
11276085 C.Baysal, and A.R.Atilgan (2001).
Elucidating the structural mechanisms for biological activity of the chemokine family.
  Proteins, 43, 150-160.  
11087354 J.Blaszczyk, E.V.Coillie, P.Proost, J.V.Damme, G.Opdenakker, G.D.Bujacz, J.M.Wang, and X.Ji (2000).
Complete crystal structure of monocyte chemotactic protein-2, a CC chemokine that interacts with multiple receptors.
  Biochemistry, 39, 14075-14081.
PDB code: 1esr
9890927 A.C.LiWang, J.J.Cao, H.Zheng, Z.Lu, S.C.Peiper, and P.J.LiWang (1999).
Dynamics study on the anti-human immunodeficiency virus chemokine viral macrophage-inflammatory protein-II (VMIP-II) reveals a fully monomeric protein.
  Biochemistry, 38, 442-453.  
  10595530 A.C.Liwang, Z.X.Wang, Y.Sun, S.C.Peiper, and P.J.Liwang (1999).
The solution structure of the anti-HIV chemokine vMIP-II.
  Protein Sci, 8, 2270-2280.
PDB code: 1vmp
10320325 H.Sticht, S.E.Escher, K.Schweimer, W.G.Forssmann, P.Rösch, and K.Adermann (1999).
Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype.
  Biochemistry, 38, 5995-6002.
PDB code: 2hcc
9618518 C.Dealwis, E.J.Fernandez, D.A.Thompson, R.J.Simon, M.A.Siani, and E.Lolis (1998).
Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 "fusin" coreceptor.
  Proc Natl Acad Sci U S A, 95, 6941-6946.
PDB code: 1a15
9622482 W.Shao, L.F.Jerva, J.West, E.Lolis, and B.I.Schweitzer (1998).
Solution structure of murine macrophage inflammatory protein-2.
  Biochemistry, 37, 8303-8313.
PDB code: 1mi2
9109648 S.Meunier, J.M.Bernassau, J.C.Guillemot, P.Ferrara, and H.Darbon (1997).
Determination of the three-dimensional structure of CC chemokine monocyte chemoattractant protein 3 by 1H two-dimensional NMR spectroscopy.
  Biochemistry, 36, 4412-4422.
PDB code: 1ncv
8631339 H.Sticht, M.Auer, B.Schmitt, J.Besemer, M.Horcher, T.Kirsch, I.J.Lindley, and P.Rösch (1996).
Structure and activity of a chimeric interleukin-8-melanoma-growth-stimulatory-activity protein.
  Eur J Biochem, 235, 26-35.
PDB code: 1rod
  8575189 A.M.Gronenborn, and G.M.Clore (1995).
Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy.
  Crit Rev Biochem Mol Biol, 30, 351-385.  
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.

 

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