We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1rg8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1rg8.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1rg8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rg8| PDB=1rg8 | SCENE= }}
{{STRUCTURE_1rg8| PDB=1rg8 | SCENE= }}
-
'''Human Acidic Fibroblast Growth Factor (haFGF-1) at 1.10 angstrom resolution (140 amino acid form)'''
+
===Human Acidic Fibroblast Growth Factor (haFGF-1) at 1.10 angstrom resolution (140 amino acid form)===
-
==Overview==
+
<!--
-
A 1.10-A atomic resolution X-ray structure of human fibroblast growth factor 1 (FGF-1), a member of the beta-trefoil superfold, has been determined. The beta-trefoil is one of 10 fundamental protein superfolds and is the only superfold to exhibit 3-fold structural symmetry (comprising 3 "trefoil" units). The quality of the diffraction data permits unambiguous assignment of Asn, Gln, and His rotamers, Pro ring pucker, as well as refinement of atomic anisotropic displacement parameters (ADPs). The FGF-1 structure exhibits numerous core-packing defects, detectable using a 1.0-A probe radius. In addition to contributing to the relatively low thermal stability of FGF-1, these defects may also permit domain motions within the structure. The availability of refined ADPs allows a translation/libration/screw (TLS) analysis of putative rigid body domains. The TLS analysis shows that beta-strands 6-12 together form a rigid body, and there is a clear demarcation in TLS motions between the adjacent carboxyl- and amino-termini. Although separate from beta-strands 6-12, the individual beta-strands 1-5 do not exhibit correlated motions; thus, this region appears to be comparatively flexible. The heparin-binding contacts of FGF-1 are located within beta-strands 6-12; conversely, a significant portion of the receptor-binding contacts are located within beta-strands 1-5. Thus, the observed rigid body motion in FGF-1 appears related to the ligand-binding functionalities.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15382229}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15382229 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15382229}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Somasundaram, T.]]
[[Category: Somasundaram, T.]]
[[Category: Beta-trefoil]]
[[Category: Beta-trefoil]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:27:34 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:09:50 2008''

Revision as of 19:09, 28 July 2008

Image:1rg8.png

Template:STRUCTURE 1rg8

Human Acidic Fibroblast Growth Factor (haFGF-1) at 1.10 angstrom resolution (140 amino acid form)

Template:ABSTRACT PUBMED 15382229

About this Structure

1RG8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

An atomic resolution structure for human fibroblast growth factor 1., Bernett MJ, Somasundaram T, Blaber M, Proteins. 2004 Nov 15;57(3):626-34. PMID:15382229

Page seeded by OCA on Mon Jul 28 22:09:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rg8"
Personal tools