PMID- 10545201
OWN - NLM
STAT- MEDLINE
DCOM- 19991221
LR  - 20061115
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 371
IP  - 2
DP  - 1999 Nov 15
TI  - Variations of sequences and amino acid compositions of proteins that sustain
      their biological functions: An analysis of the cyclophilin family of proteins.
PG  - 149-62
AB  - The sequences of the ubiquitous and phylogenetically diversified cyclophilin
      family of proteins were divided into six groups, namely, vertebrates,
      invertebrates, other metazoa, plants, fungi, and prokaryotes. These groups of
      sequences were aligned with the multiple sequence alignment program Clustal-W.
      The variations of amino acid substitutions and amino acid compositions for these 
      six groups of cyclophilins were calculated using a novel suite of
      multiple-sequence alignment analysis routines. The cyclophilins from vertebrates 
      can be divided for at least two distinct structural classes that differ from each
      other by a variable-length amino acid insert within the loop that links
      alpha-helix II and beta-strand III. A similar structural feature is also present 
      in the other groups of cyclophilins, namely, those from invertebrates, other
      metazoa, plants, and fungi. The sequences of cyclophilins from fungi and
      prokaryotes are more diversified than those from vertebrates, and their
      alterations involve structures other than the amino acid inserts within the
      loops. Variations of the hydrophobicity and bulkiness of amino acid substitutions
      of the aligned sequences were calculated for each group of cyclophilins and for
      the alignment of all the sequences. The variations have clear asymmetry that may 
      signify the need for modification of the physical properties of certain fragments
      of cyclophilins that are involved in interactions with various cellular
      components in the evolving environment.
CI  - Copyright 1999 Academic Press.
FAU - Galat, A
AU  - Galat A
AD  - Departement d'Ingenierie et d'Etudes des Proteines, DSV/CEA, Gif-sur-Yvette
      Cedex, CE-Saclay, F-91191, France.
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Bacterial Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (Plant Proteins)
RN  - 0 (Protozoan Proteins)
RN  - EC 5.2.1.8 (Peptidylprolyl Isomerase)
SB  - IM
SB  - S
MH  - Amino Acid Sequence
MH  - Animals
MH  - Bacterial Proteins/chemistry
MH  - Databases, Factual
MH  - *Evolution, Molecular
MH  - Fungal Proteins/chemistry
MH  - Invertebrates
MH  - Isomerism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Multigene Family
MH  - Peptidylprolyl Isomerase/*chemistry/*classification
MH  - Plant Proteins/chemistry
MH  - Protein Structure, Secondary
MH  - Protozoan Proteins/chemistry
MH  - Sequence Alignment/*methods
MH  - Sequence Analysis, Protein/methods
MH  - Sequence Homology, Amino Acid
MH  - Vertebrates
EDAT- 1999/11/05 00:00
MHDA- 1999/11/05 00:01
CRDT- 1999/11/05 00:00
PHST- 1999/11/05 00:00 [pubmed]
PHST- 1999/11/05 00:01 [medline]
PHST- 1999/11/05 00:00 [entrez]
AID - 10.1006/abbi.1999.1434 [doi]
AID - S0003-9861(99)91434-0 [pii]
PST - ppublish
SO  - Arch Biochem Biophys. 1999 Nov 15;371(2):149-62. doi: 10.1006/abbi.1999.1434.