PDBsum entry 2hcc

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protein links
Chemokine PDB id
Protein chain
66 a.a. *
* Residue conservation analysis
PDB id:
Name: Chemokine
Title: Solution structure of the human chemokine hcc-2, nmr, 30 structures
Structure: Human chemokine hcc-2. Chain: a. Fragment: residues 48-113 of hcc-2 precursor. Synonym: macrophage inflammatory protein 5 (mip-5), leukotactin-1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
NMR struc: 30 models
Authors: H.Sticht,S.E.Escher,K.Schweimer,W.G.Forssmann,P.Roesch, K.Adermann
Key ref:
H.Sticht et al. (1999). Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype. Biochemistry, 38, 5995-6002. PubMed id: 10320325 DOI: 10.1021/bi990065i
03-Jul-98     Release date:   13-Jul-99    
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Protein chain
Pfam   ArchSchema ?
Q16663  (CCL15_HUMAN) -  C-C motif chemokine 15
113 a.a.
66 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     immune response   1 term 
  Biochemical function     chemokine activity     1 term  


DOI no: 10.1021/bi990065i Biochemistry 38:5995-6002 (1999)
PubMed id: 10320325  
Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype.
H.Sticht, S.E.Escher, K.Schweimer, W.G.Forssmann, P.Rösch, K.Adermann.
HCC-2, a 66-amino acid residue human CC chemokine, was reported to induce chemotaxis on monocytes, T-lymphocytes, and eosinophils. The three-dimensional structure of HCC-2 has been determined by 1H nuclear magnetic resonance (NMR) spectroscopy and restrained molecular dynamics calculations on the basis of 871 experimental restraints. The structure is well-defined, exhibiting average root-mean-square deviations of 0.58 and 0.96 A for the backbone heavy atoms and all heavy atoms of residues 5-63, respectively. In contrast to most other chemokines, subtle structural differences impede dimer formation of HCC-2 in a concentration range of 0.1 microM to 2 mM. HCC-2, however, exhibits the same structural elements as the other chemokines, i.e., a triple-stranded antiparallel beta-sheet covered by an alpha-helix, showing that the chemokine fold is not influenced by quaternary interactions. Structural investigations with a HCC-2 mutant prove that a third additional disulfide bond present in wild-type HCC-2 is not necessary for maintaining the relative orientation of the helix and the beta-sheet.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19122657 R.R.Koenen, P.von Hundelshausen, I.V.Nesmelova, A.Zernecke, E.A.Liehn, A.Sarabi, B.K.Kramp, A.M.Piccinini, S.R.Paludan, M.A.Kowalska, A.J.Kungl, T.M.Hackeng, K.H.Mayo, and C.Weber (2009).
Disrupting functional interactions between platelet chemokines inhibits atherosclerosis in hyperlipidemic mice.
  Nat Med, 15, 97.  
17302442 R.L.Tuinstra, F.C.Peterson, E.S.Elgin, A.J.Pelzek, and B.F.Volkman (2007).
An engineered second disulfide bond restricts lymphotactin/XCL1 to a chemokine-like conformation with XCR1 agonist activity.
  Biochemistry, 46, 2564-2573.
PDB code: 2hdm
14984572 S.E.Escher, U.Forssmann, A.Frimpong-Boateng, K.Adermann, J.Vakili, H.Sticht, and M.Detheux (2004).
Functional analysis of chemically synthesized derivatives of the human CC chemokine CCL15/HCC-2, a high affinity CCR1 ligand.
  J Pept Res, 63, 36-47.  
11807180 E.J.Fernandez, and E.Lolis (2002).
Structure, function, and inhibition of chemokines.
  Annu Rev Pharmacol Toxicol, 42, 469-499.  
11889129 E.S.Kulo─člu, D.R.McCaslin, J.L.Markley, and B.F.Volkman (2002).
Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions.
  J Biol Chem, 277, 17863-17870.  
11470923 B.T.Seet, R.Singh, C.Paavola, E.K.Lau, T.M.Handel, and G.McFadden (2001).
Molecular determinants for CC-chemokine recognition by a poxvirus CC-chemokine inhibitor.
  Proc Natl Acad Sci U S A, 98, 9008-9013.  
11276085 C.Baysal, and A.R.Atilgan (2001).
Elucidating the structural mechanisms for biological activity of the chemokine family.
  Proteins, 43, 150-160.  
11358512 W.Shao, E.Fernandez, A.Sachpatzidis, J.Wilken, D.A.Thompson, B.I.Schweitzer, and E.Lolis (2001).
CCR2 and CCR5 receptor-binding properties of herpesvirus-8 vMIP-II based on sequence analysis and its solution structure.
  Eur J Biochem, 268, 2948-2959.
PDB code: 1hhv
  11152129 Buyong, J.Xiong, J.Lubkowski, and R.Nussinov (2000).
Homology modeling and molecular dynamics simulations of lymphotactin.
  Protein Sci, 9, 2192-2199.  
10727234 J.S.Laurence, C.Blanpain, J.W.Burgner, M.Parmentier, and P.J.LiWang (2000).
CC chemokine MIP-1 beta can function as a monomer and depends on Phe13 for receptor binding.
  Biochemistry, 39, 3401-3409.  
  11106181 J.T.Ashfield, T.Meyers, D.Lowne, P.G.Varley, J.R.Arnold, P.Tan, J.C.Yang, L.G.Czaplewski, T.Dudgeon, and J.Fisher (2000).
Chemical modification of a variant of human MIP-1alpha; implications for dimer structure.
  Protein Sci, 9, 2047-2053.  
10913244 K.L.Mayer, and M.J.Stone (2000).
NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2.
  Biochemistry, 39, 8382-8395.
PDB codes: 1eig 1eih
10707023 N.Gerber, H.Lowman, D.R.Artis, and C.Eigenbrot (2000).
Receptor-binding conformation of the "ELR" motif of IL-8: X-ray structure of the L5C/H33C variant at 2.35 A resolution.
  Proteins, 38, 361-367.
PDB code: 1qe6
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