Conservation and variability in the structures of serine proteinases of the chymotrypsin family

Arthur Lesk, William D. Fordham

Research output: Contribution to journalArticle

125 Citations (Scopus)

Abstract

The chymotrypsin-like serine proteinases are a widely divergent family of enzymes appearing in animals, bacteria and viruses. All comprise two homologous domains containing six-stranded β-barrels, with the active site between the domains. What are the structural constraints to which these proteins have been subject during their evolution, and how have the molecules explored the limits these constraints impose? We have analysed the structures of 13 widely divergent serine proteinases determined by X-ray crystallography to high resolution and well refined. We have identified the regions of the molecule that evolution has preserved both within each of the two domains and in the interdomain interface. An alignment of the sequences is presented based on structural superpositions. From this we analyse the conserved structural patterns and the interactions crucial to maintaining the structure and the active side.

Original languageEnglish (US)
Pages (from-to)501-537
Number of pages37
JournalJournal of Molecular Biology
Volume258
Issue number3
DOIs
StatePublished - May 10 1996

Fingerprint

Chymotrypsin
Serine Proteases
Sequence Alignment
X Ray Crystallography
Catalytic Domain
Viruses
Bacteria
Enzymes
Proteins
aspergillopepsin II

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Cite this

@article{1f02993d1ab94bb4a280b562eda01a54,
title = "Conservation and variability in the structures of serine proteinases of the chymotrypsin family",
abstract = "The chymotrypsin-like serine proteinases are a widely divergent family of enzymes appearing in animals, bacteria and viruses. All comprise two homologous domains containing six-stranded β-barrels, with the active site between the domains. What are the structural constraints to which these proteins have been subject during their evolution, and how have the molecules explored the limits these constraints impose? We have analysed the structures of 13 widely divergent serine proteinases determined by X-ray crystallography to high resolution and well refined. We have identified the regions of the molecule that evolution has preserved both within each of the two domains and in the interdomain interface. An alignment of the sequences is presented based on structural superpositions. From this we analyse the conserved structural patterns and the interactions crucial to maintaining the structure and the active side.",
author = "Arthur Lesk and Fordham, {William D.}",
year = "1996",
month = "5",
day = "10",
doi = "10.1006/jmbi.1996.0264",
language = "English (US)",
volume = "258",
pages = "501--537",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "3",

}

Conservation and variability in the structures of serine proteinases of the chymotrypsin family. / Lesk, Arthur; Fordham, William D.

In: Journal of Molecular Biology, Vol. 258, No. 3, 10.05.1996, p. 501-537.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Conservation and variability in the structures of serine proteinases of the chymotrypsin family

AU - Lesk, Arthur

AU - Fordham, William D.

PY - 1996/5/10

Y1 - 1996/5/10

N2 - The chymotrypsin-like serine proteinases are a widely divergent family of enzymes appearing in animals, bacteria and viruses. All comprise two homologous domains containing six-stranded β-barrels, with the active site between the domains. What are the structural constraints to which these proteins have been subject during their evolution, and how have the molecules explored the limits these constraints impose? We have analysed the structures of 13 widely divergent serine proteinases determined by X-ray crystallography to high resolution and well refined. We have identified the regions of the molecule that evolution has preserved both within each of the two domains and in the interdomain interface. An alignment of the sequences is presented based on structural superpositions. From this we analyse the conserved structural patterns and the interactions crucial to maintaining the structure and the active side.

AB - The chymotrypsin-like serine proteinases are a widely divergent family of enzymes appearing in animals, bacteria and viruses. All comprise two homologous domains containing six-stranded β-barrels, with the active site between the domains. What are the structural constraints to which these proteins have been subject during their evolution, and how have the molecules explored the limits these constraints impose? We have analysed the structures of 13 widely divergent serine proteinases determined by X-ray crystallography to high resolution and well refined. We have identified the regions of the molecule that evolution has preserved both within each of the two domains and in the interdomain interface. An alignment of the sequences is presented based on structural superpositions. From this we analyse the conserved structural patterns and the interactions crucial to maintaining the structure and the active side.

UR - http://www.scopus.com/inward/record.url?scp=0029962944&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029962944&partnerID=8YFLogxK

U2 - 10.1006/jmbi.1996.0264

DO - 10.1006/jmbi.1996.0264

M3 - Article

C2 - 8642605

AN - SCOPUS:0029962944

VL - 258

SP - 501

EP - 537

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 3

ER -