Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site. (Q54456467)

30 May 2018

title

Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site. (English)

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30 May 2018

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6

Robert Huber

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30 May 2018

9

Peter Goettig

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30 May 2018

8

Wolfram Bode

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30 May 2018

Mekdes Debela

1

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30 May 2018

Viktor Magdolen

2

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30 May 2018

Valerie Grimminger

3

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30 May 2018

Christian Sommerhoff

4

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30 May 2018

Albrecht Messerschmidt

5

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30 May 2018

Rainer Friedrich

7

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30 May 2018

language of work or name

English

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publication date

3 August 2006

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30 May 2018

Journal of Molecular Biology

published in

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30 May 2018

volume

362

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30 May 2018

issue

5

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30 May 2018

page(s)

1094-1107

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30 May 2018

1.70 A X-ray structure of human apo kallikrein 1: structural changes upon peptide inhibitor/substrate binding

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Accurate bond and angle parameters for X-ray protein structure refinement

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Kallikrein 4 is a secreted protein.

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Crystal structure and biochemical characterization of human kallikrein 6 reveals that a trypsin-like kallikrein is expressed in the central nervous system

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Characterization of hK4 (prostase), a prostate-specific serine protease: activation of the precursor of prostate specific antigen (pro-PSA) and single-chain urokinase-type plasminogen activator and degradation of prostatic acid phosphatase

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Expression and localization of tissue kallikrein mRNAs in human epidermis and appendages

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Enzymatic action of human glandular kallikrein 2 (hK2). Substrate specificity and regulation by Zn2+ and extracellular protease inhibitors

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Refined 2 A X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase. Crystallization, structure determination, crystallographic refinement, structure and its comparison with bovine trypsin

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The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution

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Interplay of human tissue kallikrein 4 (hK4) with the plasminogen activation system: hK4 regulates the structure and functions of the urokinase-type plasminogen activator receptor (uPAR).

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The expanded human kallikrein (KLK) gene family: genomic organisation, tissue-specific expression and potential functions

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Substrates of the prostate-specific serine protease prostase/KLK4 defined by positional-scanning peptide libraries

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Distinctly different gene structure of KLK4/KLK-L1/prostase/ARM1 compared with other members of the kallikrein family: intracellular localization, alternative cDNA forms, and Regulation by multiple hormones

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Refined 2.5 A X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. Crystallization, Patterson search, structure determination, refinement, structure and comparison with its [...]

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Crystal structures of uninhibited factor VIIa link its cofactor and substrate-assisted activation to specific interactions

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Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis

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Binding of Zn2+ to a Ca2+ loop allosterically attenuates the activity of factor VIIa and reduces its affinity for tissue factor

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Molecular biology of tissue kallikrein

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Enzymatic action of prostate-specific antigen (PSA or hK3): substrate specificity and regulation by Zn(2+), a tight-binding inhibitor

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Kallikrein 4 is a predominantly nuclear protein and is overexpressed in prostate cancer

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Identifiers

DOI

10.1016/J.JMB.2006.08.003

1 reference

30 May 2018

release_dbwstqtt5rhedgklyyrnlluobm

Fatcat ID

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https://api.fatcat.wiki/v0/release/dbwstqtt5rhedgklyyrnlluobm

Fatcat

reference URL

retrieved

24 November 2022

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mapped directly with Wikidata item

PubMed ID

16950394

1 reference

30 May 2018