1995
DOI: 10.1002/pro.5560040516
|View full text |Cite
|
Sign up to set email alerts
|

Crystal structure of human pepsin and its complex with pepstatin

Abstract: The three-dimensional crystal structure of human pepsin and that of its complex with pepstatin have been solved by X-ray crystallographic methods. The native pepsin structure has been refined with data collected to 2.2 A resolution to an R-factor of 19.7%. The pepsin:pepstatin structure has been refined with data to 2.0 A resolution to an R-factor of 18.5%. The hydrogen bonding interactions and the conformation adopted by pepstatin are very similar to those found in complexes of pepstatin with other aspartic p… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

1
64
0

Year Published

2003
2003
2020
2020

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 127 publications
(65 citation statements)
references
References 50 publications
1
64
0
Order By: Relevance
“…Analysis of the molecular variations may shed light on the functional differences of the three alleles. Crystal structure analysis established that an AP has three domains, the central domain, the N-terminal lobe, and the C-terminal lobe (27,37). The central domain consists of residues from three regions, the N-terminal end, the central part, and the C-terminal end.…”
Section: Discussionmentioning
confidence: 99%
“…Analysis of the molecular variations may shed light on the functional differences of the three alleles. Crystal structure analysis established that an AP has three domains, the central domain, the N-terminal lobe, and the C-terminal lobe (27,37). The central domain consists of residues from three regions, the N-terminal end, the central part, and the C-terminal end.…”
Section: Discussionmentioning
confidence: 99%
“…S3,S4). Controls using heat-denatured pepsin, active pepsin in pH 10 buffer (where pepsin has minimal activity [23] ), or active pepsin in a solution containing the inhibitor pepstatin [24] produce negligible changes in the observed color and peak positions (see Supporting Information, Fig. S3,S4).…”
mentioning
confidence: 96%
“…The peptide Iva-Val-Val constitutes part of the pepstatin A molecule and was shown to bind to the S3-S1 subsites of pepsin A when pepstatin forms a tight complex with the enzyme [20]. This peptide portion was therefore thought to bind strongly to pepsin.…”
Section: Resultsmentioning
confidence: 99%