1pph

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[[Image:1pph.gif|left|200px]]
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{{Seed}}
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[[Image:1pph.png|left|200px]]
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{{STRUCTURE_1pph| PDB=1pph | SCENE= }}
{{STRUCTURE_1pph| PDB=1pph | SCENE= }}
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'''GEOMETRY OF BINDING OF THE NALPHA-TOSYLATED PIPERIDIDES OF M-AMIDINO-, P-AMIDINO-AND P-GUANIDINO PHENYLALANINE TO THROMBIN AND TRYPSIN: X-RAY CRYSTAL STRUCTURES OF THEIR TRYPSIN COMPLEXES AND MODELING OF THEIR THROMBIN COMPLEXES'''
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===GEOMETRY OF BINDING OF THE NALPHA-TOSYLATED PIPERIDIDES OF M-AMIDINO-, P-AMIDINO-AND P-GUANIDINO PHENYLALANINE TO THROMBIN AND TRYPSIN: X-RAY CRYSTAL STRUCTURES OF THEIR TRYPSIN COMPLEXES AND MODELING OF THEIR THROMBIN COMPLEXES===
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==Overview==
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The X-ray crystal structures of the complexes formed with bovine trypsin and the N alpha-tosylated piperidides of m-amidino-, p-amidino- and p-guanidino-D,L-phenylalanine (3-TAPAP, 4-TAPAP and 4-TGPAP) were determined with data to 1.8 A resolution. The L-stereoisomer of 3-TAPAP binds as a compact entity into the active site of trypsin, with the amidino and the carbonyl groups of the central amidinophenylalanyl residue hydrogen-bonded to Gly216 of trypsin. According to modeling and energy minimization, 3-TAPAP fits perfectly in this conformation to the more restrictive thrombin active site also (Bajusz et al. (1978) Int. J. Pept. Prot. Res. 12, 217-221); the piperidine moiety extends into the cage-like S2 subsite of thrombin, but leaves room for additional substituents which might help to improve binding and pharmacological properties. In contrast, 4-TAPAP and 4-TGPAP bind only weakly and in an extended conformation to trypsin; their considerably enhanced affinities for thrombin would suggest a more compact binding to thrombin.
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(as it appears on PubMed at http://www.pubmed.gov), where 1879520 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1879520}}
==About this Structure==
==About this Structure==
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[[Category: Bode, W.]]
[[Category: Bode, W.]]
[[Category: Turk, D.]]
[[Category: Turk, D.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:20:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:00:49 2008''

Revision as of 03:00, 29 July 2008

Image:1pph.png

Template:STRUCTURE 1pph

GEOMETRY OF BINDING OF THE NALPHA-TOSYLATED PIPERIDIDES OF M-AMIDINO-, P-AMIDINO-AND P-GUANIDINO PHENYLALANINE TO THROMBIN AND TRYPSIN: X-RAY CRYSTAL STRUCTURES OF THEIR TRYPSIN COMPLEXES AND MODELING OF THEIR THROMBIN COMPLEXES

Template:ABSTRACT PUBMED 1879520

About this Structure

1PPH is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Geometry of binding of the N alpha-tosylated piperidides of m-amidino-, p-amidino- and p-guanidino phenylalanine to thrombin and trypsin. X-ray crystal structures of their trypsin complexes and modeling of their thrombin complexes., Turk D, Sturzebecher J, Bode W, FEBS Lett. 1991 Aug 5;287(1-2):133-8. PMID:1879520

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