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PDBsum entry 1lvt
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Structural protein PDB id
1lvt

 

 

 

 

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Contents
Protein chain
377 a.a.
Theoretical model
PDB id:
1lvt
Name: Structural protein
Title: Theoretical model of actin, aortic smooth muscle
Structure: Actin, aortic smooth muscle. Chain: a. Synonym: alpha-actin
Source: Gallus gallus. Chicken
Authors: R.Sagajkar
Key ref: D.B.Huang et al. (1997). Variable domain structure of kappaIV human light chain Len: high homology to the murine light chain McPC603. Mol Immunol, 34, 1291-1301. PubMed id: 9683271 DOI: 10.1016/S0161-5890(98)00002-9
Date:
29-May-02     Release date:   26-Jun-02    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P08023  (ACTA_CHICK) -  Actin, aortic smooth muscle
Seq:
Struc: 		377 a.a.
377 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.1016/S0161-5890(98)00002-9 Mol Immunol 34:1291-1301 (1997)
PubMed id: 9683271  
 
 
Variable domain structure of kappaIV human light chain Len: high homology to the murine light chain McPC603.
D.B.Huang, C.H.Chang, C.Ainsworth, G.Johnson, A.Solomon, F.J.Stevens, M.Schiffer.
 
  ABSTRACT  
 
Antibody light chains of the kappa subgroup are the predominant light chain component in human immune responses and are used almost exclusively in the antibody repertoire of mice. Human kappa light chains comprise four subgroups. To date, all crystallographic studies of human kappa light chains were carried out on proteins of the kappaI subgroup. The light chain produced by multiple myeloma patient Len. was of the kappaIV subgroup, it differed by only one residue from the germ-line gene encoded protein. The variable domain fragment of the light chain was crystallized from ammonium sulfate in space group C222(1). The crystal structure was determined by molecular replacement and refined at 1.95 A resolution to an R-factor of 0.15. Protein Len has six additional residues in its CDR1 segment compared to the kappaI proteins previously characterized. The kappaIV variable domain, Len, differs in only 23 of 113 residues from murine kappa light chain McPC603. The RMS deviation upon superimposing their alpha-carbons was 0.69 A. The CDR1 segment of the human and murine variable domains have the same length and conformation although their amino acid sequences differ in 5 out of 17 residues. Structural features were identified that could account for the significantly higher stability of the human kappaIV protein relative to its murine counterpart. This human kappaIV light chain structure is the closest human homolog to a murine light chain and can be expected to facilitate detailed structural comparisons necessary for effective humanization of murine antibodies.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20356978 C.El Hamel, A.Thierry, P.Trouillas, F.Bridoux, C.Carrion, N.Quellard, J.M.Goujon, J.C.Aldigier, J.M.Gombert, M.Cogné, and G.Touchard (2010).
Crystal-storing histiocytosis with renal Fanconi syndrome: pathological and molecular characteristics compared with classical myeloma-associated Fanconi syndrome.
  Nephrol Dial Transplant, 25, 2982-2990.  
19361523 E.G.Randles, J.R.Thompson, D.J.Martin, and M.Ramirez-Alvarado (2009).
Structural alterations within native amyloidogenic immunoglobulin light chains.
  J Mol Biol, 389, 199-210.
PDB codes: 3dvf 3dvi
18652490 D.Hu, Z.Qin, B.Xue, A.L.Fink, and V.N.Uversky (2008).
Effect of methionine oxidation on the structural properties, conformational stability, and aggregation of immunoglobulin light chain LEN.
  Biochemistry, 47, 8665-8677.  
18400753 E.M.Baden, B.A.Owen, F.C.Peterson, B.F.Volkman, M.Ramirez-Alvarado, and J.R.Thompson (2008).
Altered dimer interface decreases stability in an amyloidogenic protein.
  J Biol Chem, 283, 15853-15860.
PDB codes: 2q1e 2q20
17944486 B.O'Nuallain, A.Allen, D.Ataman, D.T.Weiss, A.Solomon, and J.S.Wall (2007).
Phage display and peptide mapping of an immunoglobulin light chain fibril-related conformational epitope.
  Biochemistry, 46, 13049-13058.  
17260953 B.O'Nuallain, A.Allen, S.J.Kennel, D.T.Weiss, A.Solomon, and J.S.Wall (2007).
Localization of a conformational epitope common to non-native and fibrillar immunoglobulin light chains.
  Biochemistry, 46, 1240-1247.  
  12964417 R.Khurana, P.O.Souillac, A.C.Coats, L.Minert, C.Ionescu-Zanetti, S.A.Carter, A.Solomon, and A.L.Fink (2003).
A model for amyloid fibril formation in immunoglobulin light chains based on comparison of amyloidogenic and benign proteins and specific antibody binding.
  Amyloid, 10, 97.  
12447901 P.A.Ramsland, and W.Farrugia (2002).
Crystal structures of human antibodies: a detailed and unfinished tapestry of immunoglobulin gene products.
  J Mol Recognit, 15, 248-259.  
11815604 P.O.Souillac, V.N.Uversky, I.S.Millett, R.Khurana, S.Doniach, and A.L.Fink (2002).
Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH.
  J Biol Chem, 277, 12666-12679.  
11815605 P.O.Souillac, V.N.Uversky, I.S.Millett, R.Khurana, S.Doniach, and A.L.Fink (2002).
Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH.
  J Biol Chem, 277, 12657-12665.  
12023282 Y.S.Kim, T.W.Randolph, F.J.Stevens, and J.F.Carpenter (2002).
Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein. Insights into transition states from pressure, temperature, and co-solute studies.
  J Biol Chem, 277, 27240-27246.  
11297418 R.Khurana, J.R.Gillespie, A.Talapatra, L.J.Minert, C.Ionescu-Zanetti, I.Millett, and A.L.Fink (2001).
Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates.
  Biochemistry, 40, 3525-3535.  
  11676295 Y.M.Lin, R.Raffen, Y.Zhou, C.S.Cassidy, M.T.Flavin, and F.J.Stevens (2001).
Amyloid fibril formation in microwell plates for screening of inhibitors.
  Amyloid, 8, 182-193.  
11112514 F.J.Stevens, P.R.Pokkuluri, and M.Schiffer (2000).
Protein conformation and disease: pathological consequences of analogous mutations in homologous proteins.
  Biochemistry, 39, 15291-15296.  
  11045631 P.R.Pokkuluri, X.Cai, G.Johnson, F.J.Stevens, and M.Schiffer (2000).
Change in dimerization mode by removal of a single unsatisfied polar residue located at the interface.
  Protein Sci, 9, 1852-1855.
PDB codes: 1qac 5lve
10557293 C.Ionescu-Zanetti, R.Khurana, J.R.Gillespie, J.S.Petrick, L.C.Trabachino, L.J.Minert, S.A.Carter, and A.L.Fink (1999).
Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy.
  Proc Natl Acad Sci U S A, 96, 13175-13179.  
  10091653 R.Raffen, L.J.Dieckman, M.Szpunar, C.Wunschl, P.R.Pokkuluri, P.Dave, P.Wilkins Stevens, X.Cai, M.Schiffer, and F.J.Stevens (1999).
Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains.
  Protein Sci, 8, 509-517.  
9739086 P.R.Pokkuluri, D.B.Huang, R.Raffen, X.Cai, G.Johnson, P.W.Stevens, F.J.Stevens, and M.Schiffer (1998).
A domain flip as a result of a single amino-acid substitution.
  Structure, 6, 1067-1073.
PDB codes: 2lve 3lve 4lve
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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