1nzk

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spinqualitylabelsall models 1nzk, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of a Multiple Mutant (L44F, L73V, V109L, L111I, C117V) of Human Acidic Fibroblast Growth Factor

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

An alternative core packing group, involving a set of five positions, has, been introduced into human acidic FGF-1. This alternative group was, designed so as to constrain the primary structure within the core region, to the same threefold symmetry present in the tertiary structure of the, protein fold (the beta-trefoil superfold). The alternative core is, essentially indistinguishable from the WT core with regard to structure, stability, and folding kinetics. The results show that the beta-trefoil, superfold is compatible with a threefold symmetric constraint on the core, region, as might be the case if the superfold arose as a result of gene, duplication/fusion events. Furthermore, this new core arrangement can form, the basis of a structural "building block" that can greatly simplify the, de novo design of beta-trefoil proteins by using symmetric structural, complementarity. Remaining asymmetry within the core appears to be related, to asymmetry in the tertiary structure associated with receptor and, heparin binding functionality of the growth factor.

Disease

Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[602115], LADD syndrome OMIM:[602115]

About this Structure

1NZK is a Single protein structure of sequence from Homo sapiens with SO4 and FMT as ligands. Full crystallographic information is available from OCA.

Reference

Accommodation of a highly symmetric core within a symmetric protein superfold., Brych SR, Kim J, Logan TM, Blaber M, Protein Sci. 2003 Dec;12(12):2704-18. PMID:14627732

Page seeded by OCA on Mon Nov 12 18:27:18 2007