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PDBsum entry 1kjs
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Cell adhesion PDB id
1kjs

 

 

 

 

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Contents
Protein chain
74 a.a. *
* Residue conservation analysis
PDB id:
1kjs
Name: Cell adhesion
Title: Nmr solution structure of c5a at ph 5.2, 303k, 20 structures
Structure: C5a. Chain: a. Synonym: complement c5a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: X.Zhang,W.Boyar,M.Toth,L.Wennogle,N.C.Gonnella
Key ref: X.Zhang et al. (1997). Structural definition of the C5a C terminus by two-dimensional nuclear magnetic resonance spectroscopy. Proteins, 28, 261-267. PubMed id: 9188742
Date:
09-Jan-97     Release date:   15-May-97    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01031  (CO5_HUMAN) -  Complement C5 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1676 a.a.
74 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
Proteins 28:261-267 (1997)
PubMed id: 9188742  
 
 
Structural definition of the C5a C terminus by two-dimensional nuclear magnetic resonance spectroscopy.
X.Zhang, W.Boyar, M.J.Toth, L.Wennogle, N.C.Gonnella.
 
  ABSTRACT  
 
The serum glycoprotein C5a, which is derived from the proteolytic cleavage of complement protein C5, has been implicated in the pathogenesis of a number of inflammatory and allergic conditions. Because C5a induces an inflammatory response upon binding to a specific receptor, structural and mutagenesis studies were carried out to gain a better understanding of this binding interaction. These studies led to the first structural definition of the C terminus of recombinant human (rh)-C5a, determined by two-dimensional nuclear magnetic resonance (NMR) spectroscopy. Our results show that the C terminus adopts an alpha-helical conformation spanning residues 69 to 74, while the core domain exists as an antiparallel alpha-helical bundle. This C-terminal helix is connected to the core by a short loop that orients Arg 74 adjacent to Arg 62. Point mutation analysis had already revealed that residues 62 and 74 significantly contribute to agonist activity and receptor binding. Correlation of the C5a tertiary structure with mutational analyses clarifies the significance of the functional and binding properties of Arg 62 and suggests that both Arg 62 and Arg 74 interact at the same binding site on the receptor.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20124699 W.J.Cook, N.Galakatos, W.C.Boyar, R.L.Walter, and S.E.Ealick (2010).
Structure of human desArg-C5a.
  Acta Crystallogr D Biol Crystallogr, 66, 190-197.
PDB codes: 3hqa 3hqb
19251703 J.H.Ippel, C.J.de Haas, A.Bunschoten, J.A.van Strijp, J.A.Kruijtzer, R.M.Liskamp, and J.Kemmink (2009).
Structure of the Tyrosine-sulfated C5a Receptor N Terminus in Complex with Chemotaxis Inhibitory Protein of Staphylococcus aureus.
  J Biol Chem, 284, 12363-12372.
PDB code: 2k3u
18227853 H.Lee, P.L.Whitfeld, and C.R.Mackay (2008).
Receptors for complement C5a. The importance of C5aR and the enigmatic role of C5L2.
  Immunol Cell Biol, 86, 153-160.  
18197169 J.D.Lambris, D.Ricklin, and B.V.Geisbrecht (2008).
Complement evasion by human pathogens.
  Nat Rev Microbiol, 6, 132-142.  
17132627 M.Pasupuleti, B.Walse, E.A.Nordahl, M.Mörgelin, M.Malmsten, and A.Schmidtchen (2007).
Preservation of antimicrobial properties of complement peptide C3a, from invertebrates to humans.
  J Biol Chem, 282, 2520-2528.  
17603557 P.N.Monk, A.M.Scola, P.Madala, and D.P.Fairlie (2007).
Function, structure and therapeutic potential of complement C5a receptors.
  Br J Pharmacol, 152, 429-448.  
17445829 P.Roversi, O.Lissina, S.Johnson, N.Ahmat, G.C.Paesen, K.Ploss, W.Boland, M.A.Nunn, and S.M.Lea (2007).
The structure of OMCI, a novel lipocalin inhibitor of the complement system.
  J Mol Biol, 369, 784-793.
PDB codes: 2cm4 2cm9
17023413 I.S.Hagemann, K.D.Narzinski, D.H.Floyd, and T.J.Baranski (2006).
Random mutagenesis of the complement factor 5a (C5a) receptor N terminus provides a structural constraint for C5a docking.
  J Biol Chem, 281, 36783-36792.  
16344483 C.K.Brown, Z.Y.Gu, Y.V.Matsuka, S.S.Purushothaman, L.A.Winter, P.P.Cleary, S.B.Olmsted, D.H.Ohlendorf, and C.A.Earhart (2005).
Structure of the streptococcal cell wall C5a peptidase.
  Proc Natl Acad Sci U S A, 102, 18391-18396.
PDB code: 1xf1
  12651630 A.Shrestha, M.Shiokawa, T.Nishimura, H.Nishiura, Y.Tanaka, N.Nishino, Y.Shibuya, and T.Yamamoto (2003).
Switch moiety in agonist/antagonist dual effect of S19 ribosomal protein dimer on leukocyte chemotactic C5a receptor.
  Am J Pathol, 162, 1381-1388.  
  11733378 Y.Shibuya, M.Shiokawa, H.Nishiura, T.Nishimura, N.Nishino, H.Okabe, K.Takagi, and T.Yamamoto (2001).
Identification of receptor-binding sites of monocyte chemotactic S19 ribosomal protein dimer.
  Am J Pathol, 159, 2293-2301.  
10336477 T.J.Baranski, P.Herzmark, O.Lichtarge, B.O.Gerber, J.Trueheart, E.C.Meng, T.Iiri, S.P.Sheikh, and H.R.Bourne (1999).
C5a receptor activation. Genetic identification of critical residues in four transmembrane helices.
  J Biol Chem, 274, 15757-15765.  
9553099 Z.Chen, X.Zhang, N.C.Gonnella, T.C.Pellas, W.C.Boyar, and F.Ni (1998).
Residues 21-30 within the extracellular N-terminal region of the C5a receptor represent a binding domain for the C5a anaphylatoxin.
  J Biol Chem, 273, 10411-10419.  
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 codes are shown on the right.

 

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