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Titolo:
THE IMMUNOGLOBULIN FOLD - STRUCTURAL CLASSIFICATION, SEQUENCE PATTERNS AND COMMON CORE
Autore:
BORK P; HOLM L; SANDER C;
Indirizzi:
EUROPEAN MOLEC BIOL LAB,MEYERHOFSTR 1 W-6900 HEIDELBERG GERMANY
Titolo Testata:
Journal of Molecular Biology
fascicolo: 4, volume: 242, anno: 1994,
pagine: 309 - 320
SICI:
0022-2836(1994)242:4<309:TIF-SC>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYSTAL-STRUCTURE; 3-DIMENSIONAL STRUCTURE; HUMAN CD4; PROTEIN STRUCTURES; MOBILE MODULES; GROWTH-HORMONE; SOLUBLE FORM; BETA-SHEETS; RESOLUTION; DOMAINS;
Keywords:
STRUCTURAL COMPARISON; SEQUENCE SIMILARITY; MOLECULAR EVOLUTION; PROTEIN FOLDING;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
55
Recensione:
Indirizzi per estratti:
Citazione:
P. Bork et al., "THE IMMUNOGLOBULIN FOLD - STRUCTURAL CLASSIFICATION, SEQUENCE PATTERNS AND COMMON CORE", Journal of Molecular Biology, 242(4), 1994, pp. 309-320

Abstract

Since the first crystal structure of an immunoglobulin revealed a modular architecture, the characteristic beta-sheet fold of the immunoglobulin domain has been found in many other proteins of diverse biological function. Here, a systematic comparison of 23 Ig domain structures with less than 25% pairwise residue identity was performed using automatic structural alignment and analysis of beta-sheet and loop topology. Sequence consensus patterns were identified for nine distinct families with at most marginal similarity to each other. The analysis reveals a common structural core of only four beta-strands (b, c, e and f), embedded in an antiparallel curled beta-sheet sandwich with a total ofthree to five additional strands (a, c', c'', d, g) and a characteristic intersheet angle. The variation in the position of the edge strands (a, c', c'', d and g) relative to the common core defines four different topological subtypes that correlate with the length of the intervening sequence between strands c and e, the most variable region in sequence. The switch of strand c' from one sheet to the other in seven-stranded domains appears to result from short c-e segments, rather thanbeing a major structural discriminator. The high degree of structuralflexibility outside the common core and the extreme variability of side-chain packing inside the core do not support a protein folding pathway common to all members of the structural class, Mutation rates of immunoglobulin-like domains in different proteins vary considerably; Disulfide bridges, thought to contribute to structural stability, are not necessarily invariant in number and location within a subclass.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 03:29:23