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Structural relationship of kappa-type light chains with AL amyloidosis: multiple deletions found in a VkappaIV protein.
Clin Exp Immunol. 1999 Dec; 118(3):344-8.CE

Abstract

Two amyloidogenic Bence Jones proteins (Am37 VkappaIV and NIG1 VkappaI) and one non-amyloidogenic protein (NIG26 VkappaIII) were characterized. The protein Am37 had four deletions when compared with the translated germ-line gene sequence: two Ser residues following position 27 (27e, 27f) in CDR1 and two amino acids Pro-44, and Tyr-49 in FR2 were deleted. A strictly conserved salt-bridge-forming amino acid, Asp-82, was replaced by the hydrophobic residue Leu. In a comparative study of amyloidogenic and non-amyloidogenic proteins, five amino acids (Ser-10, Ala-13, Ser-65, Gln-90, and Ile-106) were found to be unique to NIG1 and several other amyloidogenic proteins. Additional substitutions also occur within these proteins. These substitutions might be significant in altering protein folding as well as in contributing to their aggregation as amyloid fibrils.

Authors+Show Affiliations

Department of Neurochemistry, Tokyo Institute of Psychiatry, Tokyo, Japan. alim@comp.metro-u.ac.jpNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10594550

Citation

Alim, M A., et al. "Structural Relationship of Kappa-type Light Chains With AL Amyloidosis: Multiple Deletions Found in a VkappaIV Protein." Clinical and Experimental Immunology, vol. 118, no. 3, 1999, pp. 344-8.
Alim MA, Yamaki S, Hossain MS, et al. Structural relationship of kappa-type light chains with AL amyloidosis: multiple deletions found in a VkappaIV protein. Clin Exp Immunol. 1999;118(3):344-8.
Alim, M. A., Yamaki, S., Hossain, M. S., Takeda, K., Kozima, M., Izumi, T., Takashi, I., & Shinoda, T. (1999). Structural relationship of kappa-type light chains with AL amyloidosis: multiple deletions found in a VkappaIV protein. Clinical and Experimental Immunology, 118(3), 344-8.
Alim MA, et al. Structural Relationship of Kappa-type Light Chains With AL Amyloidosis: Multiple Deletions Found in a VkappaIV Protein. Clin Exp Immunol. 1999;118(3):344-8. PubMed PMID: 10594550.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural relationship of kappa-type light chains with AL amyloidosis: multiple deletions found in a VkappaIV protein. AU - Alim,M A, AU - Yamaki,S, AU - Hossain,M S, AU - Takeda,K, AU - Kozima,M, AU - Izumi,T, AU - Takashi,I, AU - Shinoda,T, PY - 1999/12/14/pubmed PY - 1999/12/14/medline PY - 1999/12/14/entrez SP - 344 EP - 8 JF - Clinical and experimental immunology JO - Clin Exp Immunol VL - 118 IS - 3 N2 - Two amyloidogenic Bence Jones proteins (Am37 VkappaIV and NIG1 VkappaI) and one non-amyloidogenic protein (NIG26 VkappaIII) were characterized. The protein Am37 had four deletions when compared with the translated germ-line gene sequence: two Ser residues following position 27 (27e, 27f) in CDR1 and two amino acids Pro-44, and Tyr-49 in FR2 were deleted. A strictly conserved salt-bridge-forming amino acid, Asp-82, was replaced by the hydrophobic residue Leu. In a comparative study of amyloidogenic and non-amyloidogenic proteins, five amino acids (Ser-10, Ala-13, Ser-65, Gln-90, and Ile-106) were found to be unique to NIG1 and several other amyloidogenic proteins. Additional substitutions also occur within these proteins. These substitutions might be significant in altering protein folding as well as in contributing to their aggregation as amyloid fibrils. SN - 0009-9104 UR - https://www.unboundmedicine.com/medline/citation/10594550/Structural_relationship_of_kappa_type_light_chains_with_AL_amyloidosis:_multiple_deletions_found_in_a_VkappaIV_protein_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0009-9104&date=1999&volume=118&issue=3&spage=344 DB - PRIME DP - Unbound Medicine ER -