We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1ct2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ct2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ct2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ct2| PDB=1ct2 | SCENE= }}
{{STRUCTURE_1ct2| PDB=1ct2 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE OMTKY3 P1 VARIANT OMTKY3-THR18I IN COMPLEX WITH SGPB'''
+
===CRYSTAL STRUCTURE OF THE OMTKY3 P1 VARIANT OMTKY3-THR18I IN COMPLEX WITH SGPB===
-
==Overview==
+
<!--
-
Turkey ovomucoid third domain (OMTKY3) is a canonical inhibitor of serine proteinases. Upon complex formation, the inhibitors fully exposed P1 residue becomes fully buried in the preformed cavity of the enzyme. All 20 P1 variants of OMTKY3 have been obtained by recombinant DNA technology and their equilibrium association constants have been measured with six serine proteinases. To rationalize the trends observed in this data set, high resolution crystal structures have been determined for OMTKY3 P1 variants in complex with the bacterial serine proteinase, Streptomyces griseus proteinase B (SGPB). Four high resolution complex structures are being reported in this paper; the three beta-branched variants, Ile18I, Val18I, and Thr18I, determined to 2.1, 1.6, and 1.7 A resolution, respectively, and the structure of the Ser18I variant complex, determined to 1.9 A resolution. Models of the Cys18I, Hse18I, and Ape18I variant complexes are also discussed. The beta-branched side chains are not complementary to the shape of the S1 binding pocket in SGPB, in contrast to that of the wild-type gamma-branched P1 residue for OMTKY3, Leu18I. Chi1 angles of approximately 40 degrees are imposed on the side chains of Ile18I, Val18I, and Thr18I within the S1 pocket. Dihedral angles of +60 degrees, -60 degrees, or 180 degrees are more commonly observed but 40 degrees is not unfavorable for the beta-branched side chains. Thr18I Ogamma1 also forms a hydrogen bond with Ser195 Ogamma in this orientation. The Ser18I side chain adopts two alternate conformations within the S1 pocket of SGPB, suggesting that the side chain is not stable in either conformation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10739250}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10739250 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10739250}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Beta-branched p1 residue]]
[[Category: Beta-branched p1 residue]]
[[Category: Enzyme-inhibitor complex]]
[[Category: Enzyme-inhibitor complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:05:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:19:24 2008''

Revision as of 18:19, 30 June 2008

Image:1ct2.png

Template:STRUCTURE 1ct2

CRYSTAL STRUCTURE OF THE OMTKY3 P1 VARIANT OMTKY3-THR18I IN COMPLEX WITH SGPB

Template:ABSTRACT PUBMED 10739250

About this Structure

1CT2 is a Protein complex structure of sequences from Meleagris gallopavo and Streptomyces griseus. Full crystallographic information is available from OCA.

Reference

Deleterious effects of beta-branched residues in the S1 specificity pocket of Streptomyces griseus proteinase B (SGPB): crystal structures of the turkey ovomucoid third domain variants Ile18I, Val18I, Thr18I, and Ser18I in complex with SGPB., Bateman KS, Anderson S, Lu W, Qasim MA, Laskowski M Jr, James MN, Protein Sci. 2000 Jan;9(1):83-94. PMID:10739250

Page seeded by OCA on Mon Jun 30 21:19:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ct2"
Personal tools