1trn: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1trn.gif|left|200px]]
{{Seed}}
[[Image:1trn.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1trn|  PDB=1trn  |  SCENE=  }}  
{{STRUCTURE_1trn|  PDB=1trn  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF HUMAN TRYPSIN 1: UNEXPECTED PHOSPHORYLATION OF TYROSINE 151'''
===CRYSTAL STRUCTURE OF HUMAN TRYPSIN 1: UNEXPECTED PHOSPHORYLATION OF TYROSINE 151===




==Overview==
<!--
The X-ray structure of human trypsin 1 has been determined in the presence of diisopropyl-phosphofluoridate by the molecular replacement method and refined at a resolution of 2.2 A to an R-factor of 18%. Crystals belong to the space group P4, with two independent molecules in the asymmetric unit packing as crystallographic tetramers. This study was performed in order to seek possible structural peculiarities of human trypsin 1, suggested by some striking differences in its biochemical behavior as compared to other trypsins of mammalian species. Its fold is, in fact, very similar to those of the bovine, rat and porcine trypsins, with root-mean-square differences in the 0.4 to 0.6 A range for all 223 C alpha positions. The most unexpected feature of the human trypsin 1 structure is in the phosphorylated state of tyrosine residue 151 in the present X-ray study. This feature was confirmed by mass spectrometry on the same inhibited sample and also on the native enzyme. This phosphorylation strengthens the outstanding clustering of highly negative or highly positive electrostatic surface potentials. The peculiar inhibitory behaviour of pancreatic secretory trypsin inhibitors of the Kazal type on this enzyme is discussed as a possible consequence of these properties. A charged surface loop has also been interpreted as an epitope site recognised by a monoclonal antibody specific to human trypsin 1.
The line below this paragraph, {{ABSTRACT_PUBMED_8683601}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8683601 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_8683601}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Dfp inhibited]]
[[Category: Dfp inhibited]]
[[Category: Human trypsin]]
[[Category: Human trypsin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:17:40 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:07:05 2008''

Revision as of 00:07, 28 July 2008

File:1trn.png

Template:STRUCTURE 1trn

CRYSTAL STRUCTURE OF HUMAN TRYPSIN 1: UNEXPECTED PHOSPHORYLATION OF TYROSINE 151

Template:ABSTRACT PUBMED 8683601

About this Structure

1TRN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151., Gaboriaud C, Serre L, Guy-Crotte O, Forest E, Fontecilla-Camps JC, J Mol Biol. 1996 Jun 28;259(5):995-1010. PMID:8683601

Page seeded by OCA on Mon Jul 28 03:07:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1trn&oldid=678130"