PMID- 10089404
OWN - NLM
STAT- MEDLINE
DCOM- 19990503
LR  - 20131121
IS  - 0907-4449 (Print)
IS  - 0907-4449 (Linking)
VI  - 55
IP  - Pt 1
DP  - 1999 Jan
TI  - High-resolution structures of three new trypsin-squash-inhibitor complexes: a
      detailed comparison with other trypsins and their complexes.
PG  - 139-48
AB  - An anionic trypsin from Atlantic salmon and bovine trypsin have been complexed
      with the squash-seed inhibitors, CMTI-I (Cucurbita maxima trypsin inhibitor I, P1
      Arg) and CPTI-II (Cucurbita pepo trypsin inhibitor II, P1 Lys). The crystal
      structures of three such complexes have been determined to 1.5-1.8 A resolution
      and refined to crystallographic R factors ranging from 17.6 to 19.3%. The two
      anionic salmon-trypsin complexes (ST-CPTI and ST-CMTI) and the bovine-trypsin
      complex (BT-CPTI) have been compared to other trypsin-inhibitor complexes by
      means of general structure and primary and secondary binding features. In all
      three new structures, the primary binding residue of the inhibitor binds to
      trypsin in the classical manner, but with small differences in the primary and
      secondary binding patterns. Lysine in CPTI-II binds deeper in the specificity
      pocket of bovine trypsin than lysine in other known lysine-bovine-trypsin
      complexes, and anionic salmon trypsin lacks some of the secondary binding
      interactions found in the complexes formed between squash inhibitors and bovine
      trypsin. The ST-CMTI complex was formed from the reactive-site-cleaved form of
      the inhibitor. However, well defined electron density was observed for the P1-P1'
      peptide bond, together with a hydrogen-bonding pattern virtually identical to
      those of all serine-protease-protein-inhibitor complexes, indicating a
      resynthesis of the scissile bond.
FAU - Helland, R
AU  - Helland R
AD  - Department of Chemistry, University of Tromso, N-9037 Tromso, Norway.
FAU - Berglund, G I
AU  - Berglund GI
FAU - Otlewski, J
AU  - Otlewski J
FAU - Apostoluk, W
AU  - Apostoluk W
FAU - Andersen, O A
AU  - Andersen OA
FAU - Willassen, N P
AU  - Willassen NP
FAU - Smalas, A O
AU  - Smalas AO
LA  - eng
SI  - PDB/2BTC
SI  - PDB/2STA
SI  - PDB/2STB
PT  - Comparative Study
PT  - Journal Article
DEP - 19990101
PL  - United States
TA  - Acta Crystallogr D Biol Crystallogr
JT  - Acta crystallographica. Section D, Biological crystallography
JID - 9305878
RN  - 0 (Macromolecular Substances)
RN  - 0 (Trypsin Inhibitors)
RN  - 059QF0KO0R (Water)
RN  - 9087-70-1 (Aprotinin)
RN  - EC 3.4.21.4 (Trypsin)
RN  - K3Z4F929H6 (Lysine)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Aprotinin/chemistry/genetics
MH  - Binding Sites
MH  - Cattle
MH  - Crystallography, X-Ray
MH  - Electrochemistry
MH  - Hydrogen Bonding
MH  - Lysine/chemistry
MH  - Macromolecular Substances
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - Salmo salar
MH  - Sequence Homology, Amino Acid
MH  - Trypsin/*chemistry
MH  - Trypsin Inhibitors/*chemistry/genetics
MH  - Water/chemistry
EDAT- 1999/03/25 03:01
MHDA- 2000/06/23 11:00
CRDT- 1999/03/25 03:01
PHST- 1998/04/08 00:00 [received]
PHST- 1998/08/03 00:00 [accepted]
PHST- 1999/03/25 03:01 [pubmed]
PHST- 2000/06/23 11:00 [medline]
PHST- 1999/03/25 03:01 [entrez]
AID - 10.1107/S090744499801052X [doi]
AID - S090744499801052X [pii]
PST - ppublish
SO  - Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):139-48. doi:
      10.1107/S090744499801052X. Epub 1999 Jan 1.