COMPUTER AIDED MOLECULAR MODELING OF MEMBRANE METALLOPROTEASE

Q: How can I download an article?

To download an article from SID, first log in to the site, search for the article title, and click on the 'Download Article' option.

Q: How can I download an ISI article?

To download an ISI article on SID, enter the keyword or article title in the search bar, view the relevant results, click on the desired article, and select the 'Download Article' option.

Q: How can I access the SID database?

To access the SID database, visit SID.ir, create an account, and log in to access scientific resources.

Q: Is downloading articles from SID free?

Some articles on SID are available for free, while others require payment. Details are specified on the article's page.

MAHMOUDIAN MASOUD

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Journal Paper

Paper Information

Journal: IRANIAN JOURNAL OF PHARMACOLOGY AND THERAPEUTICS (IJPT) Year:2003 | Volume:1 | Issue:2 Page(s): 30-34

Download Full-Text

View:

270

Download:

Cites:

Information Journal Paper

Title

COMPUTER AIDED MOLECULAR MODELING OF MEMBRANE METALLOPROTEASE

Author(s)

MAHMOUDIAN MASOUD

Keywords

Not Registered.

Abstract

Molecular modeling is a set of computational techniques for construction of 3D structure of a protein especially membrane bound proteins whose structures can not be elucidated using experimental techniques. These techniques has been applied in the study of membrane metalloproteases for comparing wild and mutated enzymes, docking inhibitors in the catalytic site and examination of binding pocket and mode of inhibitors binding.The present study was carried out to construct 3D structure of strmelysin-3, an important member of this family, using computer aided techniques to shed light on its biological function and provide a 3 dimensional model which could facilitate the rational design of inhibitors. The results of homology search using FASTA between the sequence of human stromelysine-3 and protein data bank showed that 1fbl has the highest similarity and this protein was used to construct the 3D structure of human stromelysin-3. The results of this modeling study showed that this enzyme has a folding structure similar to haemopexin, i.e. existence of a four-bladed structure like the flights of a dart. Zn binding and catalytic activity were described. Similar to other Zn metalloproteases His-215, His-219 and Glu-216 form the coordinates of Zn atom. It is found that the modeled human stromelysine is thermodynamically stable and agrees with biochemical data.

Multimedia

No record.

Cites

No record.

References

No record.

Cite

APA: Copy

MAHMOUDIAN, MASOUD. (2003). COMPUTER AIDED MOLECULAR MODELING OF MEMBRANE METALLOPROTEASE. IRANIAN JOURNAL OF PHARMACOLOGY AND THERAPEUTICS (IJPT), 1(2), 30-34. SID. https://sid.ir/paper/297037/en

Vancouver: Copy

MAHMOUDIAN MASOUD. COMPUTER AIDED MOLECULAR MODELING OF MEMBRANE METALLOPROTEASE. IRANIAN JOURNAL OF PHARMACOLOGY AND THERAPEUTICS (IJPT)[Internet]. 2003;1(2):30-34. Available from: https://sid.ir/paper/297037/en

IEEE: Copy

MASOUD MAHMOUDIAN, “COMPUTER AIDED MOLECULAR MODELING OF MEMBRANE METALLOPROTEASE,” IRANIAN JOURNAL OF PHARMACOLOGY AND THERAPEUTICS (IJPT), vol. 1, no. 2, pp. 30–34, 2003, [Online]. Available: https://sid.ir/paper/297037/en

Related Journal Papers

No record.

Related Seminar Papers

No record.

Related Plans

No record.

Recommended Workshops