This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ygv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ygv.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ygv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ygv| PDB=1ygv | SCENE= }}
{{STRUCTURE_1ygv| PDB=1ygv | SCENE= }}
-
'''The structure of collagen type I. Single type I collagen molecule: rigid refinment'''
+
===The structure of collagen type I. Single type I collagen molecule: rigid refinment===
-
==Overview==
+
<!--
-
The fibrous collagens are ubiquitous in animals and form the structural basis of all mammalian connective tissues, including those of the heart, vasculature, skin, cornea, bones, and tendons. However, in comparison with what is known of their production, turnover and physiological structure, very little is understood regarding the three-dimensional arrangement of collagen molecules in naturally occurring fibrils. This knowledge may provide insight into key biological processes such as fibrillo-genesis and tissue remodeling and into diseases such as heart disease and cancer. Here we present a crystallographic determination of the collagen type I supermolecular structure, where the molecular conformation of each collagen segment found within the naturally occurring crystallographic unit cell has been defined (P1, a approximately 40.0 A, b approximately 27.0 A, c approximately 678 A, alpha approximately 89.2 degrees , beta approximately 94.6 degrees , gamma approximately 105.6 degrees ; reflections: 414, overlapping, 232, and nonoverlapping, 182; resolution, 5.16 A axial and 11.1 A equatorial). This structure shows that the molecular packing topology of the collagen molecule is such that packing neighbors are arranged to form a supertwisted (discontinuous) right-handed microfibril that interdigitates with neighboring microfibrils. This interdigitation establishes the crystallographic superlattice, which is formed of quasihexagonally packed collagen molecules. In addition, the molecular packing structure of collagen shown here provides information concerning the potential modes of action of two prominent molecules involved in human health and disease: decorin and the Matrix Metallo-Proteinase (MMP) collagenase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16751282}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16751282 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16751282}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Supermolecular]]
[[Category: Supermolecular]]
[[Category: Triple-helix]]
[[Category: Triple-helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:18:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:15:04 2008''

Revision as of 13:15, 27 July 2008

Image:1ygv.png

Template:STRUCTURE 1ygv

The structure of collagen type I. Single type I collagen molecule: rigid refinment

Template:ABSTRACT PUBMED 16751282

About this Structure

1YGV is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Microfibrillar structure of type I collagen in situ., Orgel JP, Irving TC, Miller A, Wess TJ, Proc Natl Acad Sci U S A. 2006 Jun 13;103(24):9001-5. Epub 2006 Jun 2. PMID:16751282

Page seeded by OCA on Sun Jul 27 16:15:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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