Literature DB >> 9356489

A very limited number of keywords (main patterns) describes all sequences of the human variable heavy (VH) and kappa (Vkappa) domains.

I M Gelfand1, A E Kister.   

Abstract

Sequences of the variable heavy (VH) and kappa (Vkappa) domains of Ig structures were divided into 21 fragments that correspond to strands, loops, or parts of these structural units of the variable domains. Amino acid sequences of fragments (termed "words") were collected from the 1,172 human heavy and 668 human kappa chains available in the Kabat database. Statistical analysis of words of 17 fragments was performed (fragments that comprise the complementary determining regions' fragments will not be discussed in this paper). The number of different words (those with different residues in at least one position) ranged, for various fragments, from 11 to 75 in the kappa chains, and from 23 to 189 in the heavy chains. The main result of this study is that very few keywords, or main patterns of words, were necessary to describe over 90% of the sequences (no more than two keywords per fragment in the kappa and no more than five per fragment in the heavy chains). No identical keywords were found for different fragments of the variable domains. Keywords of aligned fragments of the VH and Vkappa domains were different in all but two instances. Thus, knowing the keywords, one can determine whether any given small part of a sequence belongs to a heavy or kappa chain and predict its precise localization in the sequence. In addition, by using all of the keywords obtained through analysis of the Kabat database, it was possible to describe completely the sequences of the human VH and Vkappa germ-line segments.

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Year:  1997        PMID: 9356489      PMCID: PMC25039          DOI: 10.1073/pnas.94.23.12562

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  13 in total

1.  Structural repertoire of the human VH segments.

Authors:  C Chothia; A M Lesk; E Gherardi; I M Tomlinson; G Walter; J D Marks; M B Llewelyn; G Winter
Journal:  J Mol Biol       Date:  1992-10-05       Impact factor: 5.469

2.  Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulins.

Authors:  A Tramontano; C Chothia; A M Lesk
Journal:  J Mol Biol       Date:  1990-09-05       Impact factor: 5.469

3.  Average core structures and variability measures for protein families: application to the immunoglobulins.

Authors:  M Gerstein; R B Altman
Journal:  J Mol Biol       Date:  1995-08-04       Impact factor: 5.469

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Authors:  D Beale; J Coadwell
Journal:  Int J Biochem       Date:  1989

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Authors:  E A Kabat
Journal:  Adv Protein Chem       Date:  1978

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Authors:  C Chothia; A M Lesk
Journal:  J Mol Biol       Date:  1987-08-20       Impact factor: 5.469

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Authors:  A F Williams; A N Barclay
Journal:  Annu Rev Immunol       Date:  1988       Impact factor: 28.527

Review 8.  The immunoglobulin fold. Structural classification, sequence patterns and common core.

Authors:  P Bork; L Holm; C Sander
Journal:  J Mol Biol       Date:  1994-09-30       Impact factor: 5.469

9.  Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains.

Authors:  Y Harpaz; C Chothia
Journal:  J Mol Biol       Date:  1994-05-13       Impact factor: 5.469

10.  The outline structure of the T-cell alpha beta receptor.

Authors:  C Chothia; D R Boswell; A M Lesk
Journal:  EMBO J       Date:  1988-12-01       Impact factor: 11.598

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  1 in total

1.  The sequence determinants of cadherin molecules.

Authors:  A E Kister; M A Roytberg; C Chothia; J M Vasiliev; I M Gelfand
Journal:  Protein Sci       Date:  2001-09       Impact factor: 6.725

  1 in total

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